Crystalline UDP-glycosyl transferase (MurG) and methods of use thereof

ABSTRACT

The present invention relates to crystals of the  Escherichia coli  MurG, a membrane-associated UDP-glycosyltransferase involved in peptidoglycan biosynthesis. The present invention also relates to three-dimensional atomic coordinates of the MurG protein, three-dimensional structures of the protein, and images thereof. The present invention relates to methods of crystallizing MurG proteins.

This application claims the benefit of provisional application No. 60/204,930, filed May 17, 2000.

This invention was made, in part, with U.S. governmental support under NIH grant A144854-01. The U.S. governinent has certain rights in the invention.

FIELD OF THE INVENTION

The present invention relates to crystals of the Escherichia coli MurG, a membrane-associated UDP-glycosyltransferase involved in peptidoglycan biosynthesis. The present invention also relates to three-dimensional atomic coordinates of the MurG protein, three-dimensional structures of the protein, and images thereof. The present invention also relates to the atomic coordinates and three-dimensional structures of the α-carbon backbone of the MurG protein and images thereof. The present invention further relates to the atomic coordinates and three-dimensional structures of the α-carbon backbone and conserved amino acid residue sidechains of the MurG protein and images thereof. The present invention further relates to three-dimensional atomic coordinates of the donor nucleotide binding site, the acceptor binding site, and the membrane association site of the MurG protein, three-dimensional structures of the binding domains, and images thereof. The present invention also relates to computer readable media encoded with sets of the three-dimensional coordinates of the E. coli MurG protein, the α-carbon backbone of the MurG protein, the α-carbon backbone and the conserved amino acid residue sidechains of the MurG protein, the donor nucleotide binding site, the acceptor binding site, and the membfane association site. The present invention relates to methods of crystallizing MurG proteins.

The present invention relates to models of three-dimensional structures of UDP-glycosyltransferases and, in particular, MurG proteins, based on the three-dimensional structure of crystals of the Escherichia coli MurG. The present invention also relates to models of the three-dimensional structures of the α-carbon backbone of UDP-glycosyltransferases and MurG proteins. The present invention further relates to models of the three-dimensional structure of the α-carbon backbone and conserved amino acid residue sidechains of UDP-glycosyltransferases, in particular, MurG proteins. The present invention further relates to models of the three-dimensional structures of donor nucleotide binding sites, acceptor binding sites, and membrane association sites of UDP-glycosyltransferases, in particular, MurG proteins. The present invention also relates to methods of drug design using models of this invention. The present invention further relates to compounds identified using models of the present invention that bind, inhibit or stimulate UDP-glycosyltransferases or MurG proteins. The present invention relates to compositions comprising compounds identified using the models of this invention for therapeutic or diagnositic uses. Also, the present invention relates to methods of making models of the present invention.

BACKGROUND OF THE INVENTION

The increasing frequency of resistance to existing antibiotics represents a serious public health threat. Structural and mechanistic information on essential bacterial enzymes could lead to the development of antibiotics that are active against resistant microorganisms. Both gram positive and gram negative bacterial cells are surrounded by a cross-linked carbohydrate polymer, peptidoglycan, which protects them from rupturing under high osmotic pressures. Many of the best antibiotics function by inhibiting peptidoglycan synthesis, which ultimately causes cell lysis. In recent years, intense effort has been focused on determining the structures of the enzymes that synthesize peptidoglycan. Structures of several of the early enzymes in the biosynthetic pathway have been reported (Benson et al., 1995; Bertrand et al., 1997; Fan et al., 1994; Skarzynski et al., 1996); however, the later enzymes have proven more difficult to study because both they and their substrates are membrane-associated.

MurG is the last enzyme involved in the intracellular phase of peptidoglycan synthesis (Bugg & Walsh, 1993). It catalyzes the transfer of N-acetyl glucosamine (NAG) from UDP to the C4 hydroxyl of a lipid-linked N-acetylmuramoyl pentapeptide (NAM) to form a β-linked NAG-NAM disaccharide that is transported across the cell membrane where it is polymerized and cross-linked (FIG. 1). In bacterial cells MurG associates with the cytoplasmic surface of the membrane (Bupp & van Heijenoort, 1993). However, we have found that E. coli MurG can be solubilized at high concentrations in active form (Ha et al., 1999).

The elucidation of the protein structure of a MurG protein is of importance in the identification and formulation of anti-bacterial agents. Until the discovery of the present invention, the structure and resulting mechanism by which MurG functions was not known. Thus, despite the important role of MurG in peptidoglycan synthesis, development of useful agents for treatment or diagnosis of disease was hindered by lack of structural information of the protein.

In order to obtain structural information on a MurG protein, it is important to have purified, active enzyme. The demonstration of activity requires a suitable assay, which in turn requires access to the natural substrates or analogues thereof. The study of MurG was hampered by difficulties obtaining and handling the lipid-linked NAM substrate (commonly known as Lipid I). This problem was overcome by Walker and coworkers, who developed a synthetic route to a set of substrate analogues of Lipid I that were shown to function as glycosyl acceptors in a glycosyl transfer reaction catalyzed by MurG. Some of these substrate analogues are freely water soluble, making it possible to monitor the activity of purified E. coli MurG in buffer in the absence of natural or artificial membranes or detergents.

The linear nucleic acid and amino acid sequences of E. coli MurG were reported in 1992. Subsequently, the nucleic acid and amino acid sequence of B. subtilus MurG was reported. Since then, many bacterial genomes have been sequenced and the information has been deposited in databases. Information based only on linear sequences, however, cannot accurately predict the three-dimensional structure of the protein and its functional domains.

Therefore, there is a need in the art to elucidate the three-dimensional structure of a MurG protein. One three-dimensional structure of a MurG protein can be used to construct models of other MurG proteins and to facilitate the structure determination of crystalline forms of other MurG proteins., Structures and models of MurG proteins can also be used to design proteins containing only the donor binding site or the acceptor binding site. These proteins can be used in assays, including NMR-based assays, to identify—or characterize the mode of binding of—ligands that bind in or near the vicinity of the substrates. These ligands or compounds can then be used as leads for the design of inhibitors that have therapeutic activity. Structures and models of MurG proteins can also be used in computer-based drug design.

SUMMARY OF THE INVENTION

The present invention relates to crystalline Escherichia coli MurG protein. Obtaining such crystals is an unexpected result. It is well known in the protein crystallographic art that obtaining crystals of quality sufficient for determining the structure of a protein is unpredictable. In particular, obtaining crystals of quality sufficient for determining the three-dimensional (3-D) structure of MurG has not been achievable until the crystallization of MurG as disclosed in the present application. As such, determination of the three-dimensional structure of MurG has not been possible until the discovery of the present invention. Additionally, until the discovery of the present invention, derivation of the three-dimensional structure and models of other MurG proteins has not been possible. The present inventors are also the first to define the three-dimensional structure and provide three-dimensional models for drug design for MurG proteins.

Accordingly, one object of the present invention is to provide crystals of sufficient quality to obtain a determination of the three-dimensional atomic coordinates and structures of MurG to high resolution, preferably to the resolution of less than 2.0 angstroms (A). The present invention also provides methods for producing crystalline MurG protein.

The value of the crystals of E. coli MurG protein extends beyond merely being able to obtain such crystals. The knowledge obtained concerning the MurG crystal structure, for example, has been used by the present inventors to define the heretofore unknown tertiary structure of the MurG protein and to identify the location of the glycosyl donor and glycosyl acceptor binding domains, as well as the location of the amino acid residues that are invariant in all MurG proteins. This information can be used to design inhibitors of MurG that have therapeutic utility. The atomic coordinates of E. coli MurG also are used to model the heretofore unknown tertiary structures of other MurG proteins having substantially related linear amino acid sequences, such as for MurG proteins from other microorganisms. It is anticipated that homology models can be constructed even from amino acid sequences with relatively low homology because the present inventors have identified the location of the invariant amino acid residues in MurG. The relative spatial orientations of such residues is expected to be conserved in all MurG proteins.

Comparison of nucleic acid and amino acid sequences of MurG proteins indicates that the linear amino acid sequences can vary significantly. Homology between MurG proteins from different microorganisms varies from less than 30% to greater than 90%, reflecting the evolutionary relationship between the organisms. The low homology between distantly related MurG homologues is not believed to reflect significantly different folded structures. It is well known that many amino acid sequences are capable of adopting the same general fold. E. coli MurG contains an alpha/beta folding pattern, one of the most common folds known in proteins. It is likely that all MurG homologues contain a similar alphalbeta fold despite the differences in the linear amino acid sequences. What gives these proteins their identity is not the general fold, but the specific details—i.e., the presentation of certain amino acids on the folded structure. The present inventors have identified the location in E. coli MurG of a set of residues that are invariant in all MurG homologues. It is to be expected that these residues would adopt a similar spatial location with respect to the folded structure in all MurG homologues. Therefore, these invariant residues, which have been selected by evolution as the critical residues for the binding and catalytic function of the protein, provide essential information on the location of the active site and on critical contacts to the substrates/products. They also serve as constraints that make it possible to, predict the three-dimensional structures even of distantly related MurG homologues. Thus, knowledge of the three-dimensional structure of the E. coli MurG protein has provided a starting point for investigation into the structure of all MurG proteins.

Accordingly, a object of the present invention is to provide information regarding the atomic coordinates and three-dimensional structures of (1) the MurG protein, (2) the α-carbon backbone of the MurG protein, (3) the α-carbon backbone and conserved amino acid residues of the MurG protein, (4) the donor nucleotide binding site, (5) the acceptor binding site, and (6) the membrane association site MurG proteins.

It is also an object of this invention to solve the three-dimensional structure of UDP-glycosyltransferases, in particular target NTURG proteins, and to determine their structure and/or atomic coordinates. Further, it is an object of this invention to use the structure or atomic coordinates of the E. coli MurG crystal to solve the structure of different MurG protein crystals, or a crystal of a mutant protein, homolog or co-complex of MurG.

The present invention relates to models of three-dimensional structures of UDP-glycosyltransferases, in particular MurG proteins, based on the atomic coordinates of crystalline E. coli MurG protein.

It is a further object of this invention to provide, UDP-glycosyltransferase enzyme mutants characterized by one or more different properties as compared with wild-type MurG. These properties include altered surface charge, increased stability to subunit dissociation, altered substrate specificity or higher specific activity. MurG mutants are useful to identify those amino acids that are most important for the enzymatic activity of MurG. This information, in turn, allows the design of improved inhibitors of MurG as compared with peptidic MurG inhibitors.

Another object of the present invention is to provide computer readable mediums encoded with a set of three-dimensional coordinates of the E. coli MurG protein, the c-carbon backbone of the MurG protein, the c-carbon backbone and conserved amino acid residues of the MurG protein, and the nucleotide donor binding site, the acceptor binding site, the membrane association site of the MurG protein.

Another embodiment of the present invention provides three-dimensional and two-dimensional computer images of the three-dimensional structure of MurG protein, the α-carbon backbone of the MurG protein, the α-carbon backbone and conserved amino acid residues of the MurG protein, and the nucleotide donor binding site, the acceptor binding site, the membrane association site of the MurG protein.

The knowledge of the three-dimensional structure of MurG also provides a means for designing proteins that have altered beneficial functions by analyzing the structure and interactions between individual amino acids of the protein. For example, the present inventors have shown that E. coli MurG consists of two domains separated by a cleft.

Noncovalent interactions between the two domains are not extensive. The present inventors have shown that the domains fold independently and can, therefore, be expressed independently either alone or as part of a recombinant protein containing the acceptor binding site from one MurG homologue and the donor binding site from another MurG homologue. It would be expected that the domains of other MurG proteins could also be expressed independently, either alone or as chimaeras with other MurG domains. Independently expressed domains of the protein are useful for discovering ligands that bind to the individual domains.

The knowledge of the three-dimensional structure of E. coli MurG protein and models of other MurG proteins also provides a means for designing and producing compounds that regulate, inhibit or antagonize functions of the MurG protein (i.e., structure based drug design). For example, chemical compounds can be designed to block binding of UDP-GlcNAc to a MurG protein using various computer programs and models.

It is also an object of this invention to use the structure coordinates and atomic details of MurG, or its mutants or homologues or co-complexes, to design, evaluate computationally, synthesize and use inhibitors of MurG that avoid the undesirable physical and pharmacologic properties of peptidic MurG inhibitors.

Another embodiment of the present invention is a composition comprising MurG protein in a crystalline form.

Yet another embodiment of the present invention is a method for producing crystals of MurG, comprising combining MurG protein in a suitable buffer with a suitable amount of a reservoir buffer containing a detergent, and inducing crystal formation to produce said MurG crystals.

BRIEF DESCRIPTION OF THE DRAWINGS

The patent or application file contains at least one drawing executed in color. Copies of this patent or patent application publication with color drawings will be provided by the Office upon request and payment of the necessary fees.

FIG. 1. Pathway for peptidoglycan biosynthesis.

FIG. 2. Overall architecture of MurG. A. Stereo view of the MurG structure. The N domain is shown in purple; the C domain is shown in green. The figure was generated with the programs MOLSCRIPT (Klaulis, 1991) and RASTER31) (Merrit & Murphy, 1994). B. Topology diagram of MurG.

FIG. 3. Identification of critical residues in MurG and related glycosyltransferases. A. Sequence alignment of E. coli MurG with homologs from seven other bacterial strains, deliberately chosen to represent a disparate group of organisms. The secondary structure of E. coli MurG is shown above the sequences. Gaps mapping to the loop regions of E. coli MurG suggest that some sequences include other structural elements. Residues highlighted in blue are invariant among the eighteen MurG sequences available. Residues highlighted in yellow are identical in 85% of the eighteen homologs, while in the remaining 15%, only closely related amino acid substitutions are found. Highly conserved residues that do not meet the stringent criteria established for highlighting are shown in the consensus sequence. A consensus motif for UDP-glucuronosyltransferases is also shown. Numbering is with respect to the overexpressed E. coli MurG construct, which contains an additional N-terininal methionine. B. Mapping of the G loops and other highlighted residues from FIG. 3 a in red on the MurG structure. Side chains for highly conserved residues are also shown. C. Model for the proposed UDP-binding subdomain found in many UDP-glycosyltransferases based on the E. coli MurG structure. Conserved residues in UDP-glucuronosyltransferases are highlighted in red. Side chains are shown for residues that are located near the cleft and may be involved in substrate binding. The glutamate residue is proposed to interact with the ribose sugar. The dotted loop varies in length within the MurG family and in other UDP-sugar transferases, but the N and Q on the following helix are invariant. Note that the UDPglucuronosyltransferases contain a conserved D preceding the Q, which is not shown on this model.

FIG. 4. Structural analysis of the substrate binding pockets in MurG. A. Structural comparison between the C-terminal domain of phage T4 β-glucosyltransferase (left) and the C-terminal domain of E. coli MurG (right). The aligned six β-strands are magenta, the aligned α-helices are orange, and the other structural elements are blue. In β-glucosyltransferase, key residues involved in UDP binding are highlighted in yellow. The analogous residues in MurG are also highlighted in yellow. B. A close-up view of the proposed donor binding pocket in the MurG C domain with the docked UDP-GlcNAc. Conserved residues in MurG are colored magenta. The carbonyl oxygen of residue 1245 is shown in red, and its backbone nitrogen is shown in blue. C. The surface of E. coli MurG. The G loops and other conserved residues in MurG are colored magenta. The proposed membrane binding interface is also highlighted with hydrophobic residues in yellow and positively charged residues in blue.

DEFINITIONS

It is to be noted that the term “a” or “an” entity refers to one or more of that entity; for example, a compound refers to one or more compounds or at least one compound. As such, the terms “a” (or “an”), “one or more”, and “at least one” can be used interchangeably herein.

It is also to be noted that the terms “comprising”, “including” and “having” can be used interchangeably. Furthermore, a compound “selected from the group consisting of” refers to one or more of the compounds in the list that follows, including mixtures (i.e., combinations) of two or more of the compounds.

According to the present invention, an isolated, or pure, protein, is a protein that has been removed form its natural milieu. As such, “isolated” and “biologically pure” do not necessarily reflect the extent to which the protein has been purified. An isolated protein of the present invention can be obtained from its natural source, can be produced using recombinant DNA technology or can be produced by chemical synthesis.

It is also to be noted that the terms “tertiary” and “three-dimensional” can be used interchangeably.

It is also to be noted that reference to a “MurG protein” can also be recited as “MurG” and such terms can be used to refer to the complete MurG protein, a portion of the MurG protein, such as a polypeptide.

The following terms are also used herein:

The term “naturally occurring amino acids” means the L-isomers of the naturally occurring amino acids. The naturally occurring amino acids are glycine, alanine, valine, leucine, isoleucine, serine, methionine, threonine, phenylalanine, tyrosine, tryptophan, cysteine, proline, histidine, aspartic acid, asparagine, glutamic acid, glutamine, gamma-carboxyglutamic acid, arginine, omithine and lysine. Unless specifically indicated, all amino acids referred to in this application are in the L-form.

The terin “unnatural amino acids” means amino acids that are not naturally found in proteins. Examples of unnatural amino acids used herein, include racemic mixtures of selenocysteine and selenomethionine. In addition, unnatural amino acids include the D or L forms of nor-leucine, para-nitrophenylalanine, homophenylalanine, parafluorophenylalanine, 3-amino-p2-benzylpropionic acid, homoarginine, and D-phenylalanine.

The term “positively charged amino acid” includes any naturally occurring or unnatural amino acid having a positively charged side chain under normal physiological conditions. Examples of positively charged naturally occurring amino acids are arginine, lysine and histidine.

The term “negatively charged amino acid” includes any naturally occurring or unnatural amino acid having a negatively charged side chain under normal physiological conditions. Examples of negatively charged naturally occurring amino acids are aspartic acid and glutamic acid.

The term “hydrophobic amino acid” means any amino acid having an uncharged, nonpolar side chain that is relatively insoluble in water. Examples of naturally occurring hydrophobic amino acids are alanine, leucine, isoleucine, valine, proline, phenylalanine, tryptophan and methionine.

The term “hydrophilic amino acid” means any amino acid having an uncharged, polar side chain that is relatively soluble in water. Examples of naturally occurring hydrophilic amino acids are serine, threonine, tyrosine, asparagine, glutamine, and cysteine.

The term “MurG” refers to a UDP-glycosyltransferase that has a two domain strucuture, where each domain contains a set of invariant residues as shown in FIG. 3 a, including any mutant, homologue or co-complex or any similar enzyme that catalyzes the transfer of N-acetylglucosamine (GlcNAc) from UDP to the C4 hydroxyl of the lipidlinked MurNAc pentapeptide.

The term “mutant” refers to a MurG polypeptide, i.e., a polypeptide displaying the biological activity of a wild-type MurG, characterized by the replacement of at least one amino acid from the wild-type, E. coli MurG sequence according to Ikeda, et al., Nucleic Acids Res. 1990, and Mengin-LeCreuix et al., Nucleic Acids Res. 1990. Such a mutant may be prepared, for example, by expression of MurG cDNA previously altered in its coding sequence by PCR-based mutagenesis method.

MurG mutants may also be generated by site-specific incorporation of unnatural amino acids into MurG proteins using the general biosynthetic method of Noren, C. J., et al., Science, 244, pp. 182-188 (1989). In this method, the codon encoding the amino acid of interest in wild-type MurG is replaced by a “blank” nonsense codon, TAG, using oligonucleotide-directed mutagenesis (described in detail, infra). A suppressor tRNA directed against this codon is then chemically aminoacylated in vitro with the desired unnatural amino acid. The aminoacylated tRNA is then added to an in vitro translation system to yield a mutant MurG enzyme with the site-specific incorporated unnatural amino acid.

Selenocysteine or selenomethionine may be incorporated into wild-type or mutant MurG by expression of MurG-encoding cDNAs in auxotrophic E. coli strains. Hendrickson, W. A. et al., EMBO J., 9(5), pp. 1665-1672 (1990). In this method, the wild-type or mutagenized MurG cDNA may be expressed in a host organism on a growth medium depleted of either natural cysteine or methionine (or both) but enriched in selenocysteine or selenomethionine (or both).

The term “altered surface charge” means a change in one or more of the charge units of a mutant polypeptide, at physiological pH, as compared to wild-type MurG. This is preferably achieved by mutation of at least one amino acid of wild-type MurG to an amino acid comprising a side chain with a different charge at physiological pH than the original wild-type side chain.

The change in surface charge is determined by measuring the isoelectric point (pI) of the polypeptide molecule containing the substituted amino acid and comparing it to the isoelectric point of the wild-type MurG molecule.

The term “altered substrate specificity” refers to a change in the ability of a mutant MurG to cleave a substrate as compared to wild-type MurG.

The “kinetic form” of MurG refers to the condition of the enzyme in its free or unbound form or bound to a chemical entity at either its active site or accessory binding site.

A “competitive” inhibitor is one that inhibits MurG activity by binding to the same kinetic form of MurG as its substrate binds-thus directly competing with the substrate for the active site of MurG. Competitive inhibition can be reversed completely by increasing the substrate concentration.

An “uncompetitive” inhibitor is one that inhibits MurG by binding to a different kinetic form of the enzyme than does the substrate. Such inhibitors bind to MurG already bound with the substrate and not to the free enzyme. Uncompetitive inhibition cannot be reversed completely by increasing the substrate concentration.

A “non-competitive” inhibitor is one that can bind to either the free or substrate bound form of MurG.

Those of skill in the art may identify inhibitors as competitive, uncompetitive or non-competitive, by computer fitting enzyme kinetic data using standard equations according to Segel, I. H., Enzyme Kinetics, J. Wiley & Sons, (1975). It should also be understood that uncompetitive or non-competitive inhibitors apcording to this invention may bind to the accessory binding site.

The term “homolog” means a protein having at least 25% amino acid sequence identity with MurG or any functional part of MurG, and including certain invariant amino acid residues corresponding to G14, G15, G18, H19, G104, H124, E125, G190, G191, S192, G194, A195, R261, G263, A264, E269, P281, Q289, N292 and A293 (as numbered in the E. coli MurG sequence set forth in FIG. 3 a) and also including three glycine rich loops. A homolog may contain some or all of the invariant residues.

The term “co-complex” means MurG or a mutant or homologue of MurG in covalent or non-covalent association with a chemical entity or compound.

The term “associating with” refers to a condition of proximity between a chemical entity or compound, or portions thereof, and a MurG molecule or portions thereof. The association may be non-covalent—wherein the juxtaposition is energetically favored by hydrogen bonding or van der Waals or electrostatic interactions—or it may be covalent.

The term “.beta.-sheet” refers to the conformation of a polypeptide chain stretched into an extended zig-zig conformation. Portions of polypeptide chains that run “parallel” all run in the same direction. Polypeptide chains that arc “antiparallel” run in the opposite direction from the parallel chains.

The terms “atomic coordinates” or “structure coordinates” refer to mathematical coordinates derived from mathematical equations related to the patterns obtained on diffraction of a monochromatic beam of X-rays by the atoms (scattering centers) of a MurG molecule in crystal form. The diffraction data are used to calculate an electron density map of the repeating unit of the crystal. The electron density maps are used to establish the positions of the individual atoms within the unit cell of the crystal.

The term “heavy atom derivatization” refers to the method of producing a chemically modified form of a crystal of MurG. In practice, a MurG crystal is soaked in a solution containing heavy metal atom salts, or organometallic compounds, e.g., lead chloride, gold thiomalate, thimerosal, uranyl acetate or mercuric chloride, which can diffuse through the crystal and bind to the surface of the protein. The location(s) of the bound heavy metal atom(s) can be deetermined by X-ray diffraction analysis of the soaked crystal. This information, in turn, is used to generate the phase information used to construct three-dimensional structure of the enzyme. Blundel, T. L. and N. L. Johnson, Protein Crystallography, Academic Press (1976).

Those of skill in the art understand that a set of structure coordinates determined by X-ray crystallography is not without standard error. For the purpose of this invention, any set of structure coordinates for MurG or MurG homologues or MurG mutants that have a root mean square deviation of protein backbone atoms (N, C.alpha., C and 0) of less than 0.75 Å when superimposed—using backbone atoms—on the structure coordinates listed in Table 1, Table 2 or Table 3 shall be considered identical.

The term “unit cell” refers to a basic parallelepiped shaped block. The entire volume of a crystal may be constructed by regular assembly of such blocks. Each unit cell comprises a complete representation of the unit of pattern, the repetition of which builds up the crystal.

The term “space group” refers to the arrangement of symmetry elements of a crystal.

The term “molecular replacement” refers to a method that involves generating a preliminary model of a MurG crystal whose structure coordinates are unknown, by orienting and positioning a molecule whose structure coordinates are known (e.g., MurG coordinates from Table 1, 2, or 3) within the unit cell of the unknown crystal so as best to account for the observed diffraction pattern of the unknown crystal. Phases can then be calculated from this model and combined with the observed amplitudes to give an approximate Fourier synthesis of the structure whose coordinates are unknown. This, in turn, can be subject to any of the several forms of refinement to provide a final, accurate structure of the unknown crystal. Lattman, K., “Use of the Rotation and Translation Functions”, in Methods in Enzymology, 115, pp. 55-77 (1985); M. G. Rossmann, ed., “The Molecular Replacement Method”, Int. Sci. Rev. Ser., No. 13, Gordon & Breach, New York, (1972). Using the structure coordinates of MurG provided by this invention, molecular replacement may be used to determine the structure coordinates of a crystalline mutant or homologue of MurG or of a different crystal form of MurG.

DETAILED DESCRIPTION OF THE INVENTION

The present invention relates to the discovery of the three-dimensional structure of the crystalline form of the E. coli MurG protein, models of such three-dimensional structures, a method of structure based drug design using such structures, methods to identify ligands or compounds that interact or bind with such structures, the compounds identified by such methods, and the use of such compounds in therapeutic compositions.

More particularly, the present invention relates to novel crystals of E. coli MurG protein, methods of production of such crystals, three-dimensional coordinates of MurG protein, MurG structures and models derived from the E. coli MurG structure, and uses of such structures and models to derive other MurG structures and in ligand discovery and drug design strategies.

The present invention also relates to three-dimensional structures and coordinates of the donor nucleotide binding site, the acceptor binding site, and the membrane association site of the MurG protein, structures and models of the binding sites, and uses of such structures and models to derive the binding sites of other MurG proteins and in drug design strategies.

Solely for ease of explanation, the description of the invention is divided into the following sections: (1) crystals of MurG protein; (2) methods of crystallization; (3) three-dimensional crystal coordinates and structure of E. coli MurG; (4) three-dimensional coordinates and structure of the donor nucleotide binding site of MurG; (5) coordinates and structure of the acceptor binding site of MurG; (5) three-dimensional coordinates and structure of the membrane association site; (6) two-dimensional and three-dimensional images of the protein, α-carbon backbone, α-carbon backbone with conserved amino acid residues, and binding sites; and (7) computer readable mediums comprising the three-dimensional coordinates of the MurG protein, α-carbon backbone, α-carbon backbone with conserved amino acid residues, and binding sites; (8) images of structures of MurG protiensand binding sites; (9) models of MurG proteins and binding sites thereof and methods of using the structure of MurG to determine the structures of other MurG proteins and binding sites; (10) structure based drug design using models of MurG protein and binding site structures; (11) compounds derived from structure based drug design; and (12) therapeutic compositions using drugs designed from structure based drug design.

Crystals

One embodiment of the present invention includes a pomposition comprising a MurG protein in a crystalline form (i.e., MurG crystals). As used herein, the terms (crystalline MurG” and “MurG crystal” both refer to crystallized MurG protein and are intended to be used interchangeably. More particularly, an embodiment of the present invention includes a composition comprising an E. coli MurG protein in a crystalline form. Preferably, a crystalline MurG is produced using the crystal formation method described herein, in particular according to the method disclosed in Example 1. A MurG crystal of the present invention comprises any crystal structure and preferably precipitates as a triclinic crystal. Preferably, a composition of the present invention includes MurG crystal molecules arranged in a crystalline manner in a P1 space group with two molecules per assymmetric unit so as to form a unit cell of dimensions a-60.613 Å, b=66.356 Å, c=67.902 Å, α=64.294, β=83.520, γ=65.448. A preferred crystal of the present invention provides X-ray diffraction data for determination of atomic coordinates to a resolution of about 3.0 Å, preferably to about 2.4 Å, and more preferably to about 1.8 Å.

Another embodiment of the present invention includes crystalline MurG protein co-crystallized with a donor nucleotide or substrate or substrate analog. Preferably, a donor nucleotide is UDP or UDP-GlcNAc (UDP-N-acetylglucosamine) or an analog thereof. The substrate or substrate analog is preferably Lipid I or Lipid II or analogs of Lipid I or Lipid II. More specifically, Lipid I and II analogs are as described in PCT/US99/02187, published as WO99/38958 and U.S. Provisional Application No. 60/122,966 filed Mar. 3, 1999 and 60/137,696 filed Jun. 4, 1999, and International Application No. PCT/US00/05554 entitled “Bacterial transglycosylases: Assays for monitoring the activity using Lipid II substrate analogs and methods for discovering antibiotics,” all incorporated herein by reference in their entirety.

Included in the present invention, a variety of MurG proteins from numerous organisms can be used to prepare MurG crystals, including but not limited to, microorganisms such as bacteria, higher-order bacteria, thermal stable bacteria, spirochetes, small pathogenic organisms, fungi, protozoa, cyanobacteria, and trypanosomes. More particularly, bacteria such as but not limited to, Escherichia coli, Bacillus subtilis, Aquefe-x aeolicus, Borrelia burgdorferi, Chlamydia pneumoniae, Chlamydia trachomatis, Enterococcus jaecais, Enterococcus hirae, Haemophilus influenzae, Helicobacter pylori J99, Helicobacter pylori, Mjrobacterium tuberculosis, Porphyromonas gingivalis, Rickettsia prowazekii, Streptomyces coelicolor, Streptomyces collinus, Streptococcus pneumoniae, Synechocystis sp. (strain PCC6803), Thermotoga maritime, and Treponemapallidum.

In another embodiment of the present invention, the MurG proteins or fragments thereof, mutants or homologs are expressed in, for example, an E. coli host cell for use expressing sufficient quantities of sufficiently purified protein to form crystals. The present inventors have demonstrated that it is possible to express Enterococcus. jaecalis MurG in E. coli cells—so the MurG proteins from many organisms can be cloned into expression vectors suitable for expression in E. coli cells. This would facilitate obtaining sufficient quanitites of isolated or purified MurG proteins. The expression of E. jaecalis MurG protein in E. coli host cells is performed, for example, by expressing the E. jaecalis MurG gene cloned into a pET21b expression vector and transformed into an E. coli host cell. The MurG protein is over-expressed with a C-terminal his tag (LEHHHHHH) which allows the protein to be purified using a His-tag affinity column. The protein is then crystallized and the atomic coordinates are determined using X-ray diffraction and methods known to those skilled in the art.

It is another embodiment of the present invention to provide for the construction and expression of chimaeric MurG proteins to enable the crystallization and determination of the three-dimensional coordinates of such chimeras. For example, if there are problems obtaining or crystallizing MurGs from other organisms, the present invention provides information that makes it possible to make chimaeric proteins containing the donor or acceptor binding site from E. coli MurG and the corresponding acceptor or donor binding site from another organism. Chimaeric proteins could be easier to express, handle, or crystallize. For example, we have found that E. faecalis MurG is more difficult to solubilize that E. coli MurG (requiring more detergent). It is believed that the problems are related to the acceptor binding domain having a stronger affinity for the bacterial membranes. To overcome this problem, one can attach the donor binding domain of E. faecalis to the E. coli acceptor binding site and determine structure to see details of E. faecalis donor binding domain.

According to the present invention, crystalline MurG can be used to determine the ability of a chemical compound to bind to a MurG protein in a manner predicted by a structure based drug design method of the present invention. Preferably, a MurG crystal is soaked in a solution containing a chemical compound of the present invention. Binding of the chemical compound to the crystal is then determined by methods standard in the art. Thereby, the co-crystal of MurG and a compound of interest is determined.

Methods of Crystallization

The present invention includes a method for producing crystals of MurG proteins, comprising: combining MurG protein with a reservoir solution and inducing crystal formation to produce MurG crystals. Another embodiment of the present invention, a method for producing crystals of MurG protein comprises combining MurG protein with UDP-GlcNAc in a 1:3 ratio and with a reservoir solution and inducing crystal formation to produce MurG crystals.

Preferably, crystals of MurG are formed using a solution containing a range of MurG protein from about 1 mg/ml to about 20 mg/ml, more preferably above 5 mg/ml, limited only by the solubility of the protein, which may vary depending on the specific amino acid sequence.

A reservoir solution contains the buffer, the precipitant, and additives if necessary. A suitable reservoir buffer of the present invention comprises NaMES (2-[N-morpho]inolethanesulfonic acid, sodium salt) buffer, NaHEPES (N-[2-hydroxyethyl]piperazine-N′-[2-ethanesulfonic acid, sodium salt) buffer, Tris (tris[hydroxymethyl]aminomethane) buffer, and any buffer which has the PKa between 5.5 and 8.0. A suitable NaMES buffer solution has a pH range from about 5.6-6.5. Most preferably, the NaMES buffer has a pH of about 6.5. The precipitant comprises ammonium sulfate, saturated sodium and potassium tartrate and polyethylene glycol. A suitable concentration of ammonium sulfate can range from 0.8 M to 1.5 M. Most preferably, the ammonium sulfate concentration is about 0.96 M. A suitable additive comprises detergents like Triton X-100 and n-octyl-beta-glucoside. The concentration of Triton X-100 can range from 0.1% to 1%. Most preferably, the concentration of Triton X-100 is 0.4%.

In a preferred embodiment, MurG crystals are produced by a method comprising concentrating MurG protein in a buffer solution, mixing the protein concentrate with UDP-GlcNAc in a 1:3 molar ratio, mixing equal volumes of protein solution with a reservoir solution, and inducing crystal formation to produce MurG crystals.

In a particular embodiment of the invention, MurG crystals are produced by a method comprising concentrating MurG protein to 10 mg/ml in a buffer of 20 mM Tris-HCl, pH 7.9/150 mM NaCl and 50 mM EDTA; mixing the protein concentrate with UDP-GlcNAc in a 1:3 molar ratio; mixing equal volumes of protein solution with a reservoir solution comprising (0.1 M NaMES, pH 6.5, 0.96 M (NH₄)₃SO₄, 0.4% TRITON® X-100, and 10 mM dithiolthreitol (DTT)), and inducing crystal formation using hanging drop vapor-diffusion. This preferred method is described in greater detail in Example 1.

Supersaturated solutions of MurG protein can be induced to crystallize by several methods including, but not limited to, vapor diffusion, liquid diffusion, batch crystallization, constant temperature and temperature induction or a combination thereof. Preferably, supersaturated solutions of MurG protein are induced to crystallize by vapor diffusion (i.e., hanging drop method). In a vapor diffusion method, a MurG protein solution is combined with a reservoir solution of the present invention that will cause the MurG protein solution to become supersaturated and form MurG crystals at a constant temperature. Vapor diffusion is preferably performed under a controlled temperature in the range of from about 15° C. to about 30° C., more preferably from about 20° C. to about 25° C., and most preferably at a constant temperature of about 22° C.

In another preferred embodiment, the present invention includes a method to produce crystals of MurG protein comprising the steps of: (a) preparing an about 10 mg/ml solution of MurG protein in a Tris-HCl buffer, (mixing UDP-GlcNAc with the Mur-G protein solution in a 3:1 molar ratio, (c) dropping 2 μl droplet of this protein sample onto a coverslip, (d) adding an equal volume of reservoir solution to this droplet and inverting this over a well containing about 1 ml of the reservoir solution; and (e) incubating until crystals of MurG form.

Any isolated MurG protein can be used with the present method. An isolated MurG protein can be isolated from its natural milieu or produced using recombinant DNA technology (e.g., polymerase chain reaction (PCR) amplification, cloning) or chemical synthesis. To produce recombinant MurG protein, a nucleic acid molecule encoding a MurG protein can be inserted into any vector capable of expressing the nucleic acid in a host clell. Suitable and preferred nucleic acid molecules to include in recombinant vectors of the present invention are as disclosed herein. Such suitable and preferred nucleic acid molecules include numerous MurG encoding genes that have been isolated to date, and that will be isolated in the future. A preferred nucleic acid molecule of the present invention encodes a homologue of MurG. Homologues of MurG can be recognized by the presence of certain conserved amino acid residues or sequences.

A sequence alignment for six MurG sequences is shown in FIG. 3A. Highlighted residues include those that are invariant or almost invariant across all MurG proteins. A nucleic acid molecule of the present invention can encode any portion of a MurG protein, preferably a full-length MurG protein or either of the two domains. A more preferred nucleic acid molecule to include in a recombinant vector, and particularly in a recombinant molecule, includes a nucleic acid molecule encoding a protein having the amino acid sequence represented by amino acid sequences of MurG proteins as deposited in the NCBI database and are identified with Accession Nos. CAB51993, A71316, E70579, C71699, F70195, A43727, JC1275, BVECMG, CEECAM, 083535, Q9ZK59, CAB85280, AAF39020, BAA18775, AAD26629, CAB73295, P37585, Q9ZHA9, Q9ZHDC0, Q9ZBA5, Q9X4H4, Q9WY74, P74657, O06224, Q9Z702, O84766, O69552, O67238, O51708, O25770, O07670, O07109, P45065, CAB66324, AAC68356, AAF06830, P18579, P17443, P17952, P16457, P07862, AAE23178, AAD53936, CAA18668, CAA38869, CAA38868, CAA38867, CAA38866, AAD08196, BAA01453, BAA01455, BAA01454, AAD19042, CAA45558, CAA74235, AAD10537, AAD06652, AAC95450, CAA14869, AAC73201, AAC65509, AAC67113, AAC45636, CAB08640, AAC22793, AAC07193, BAA24357, CAB13395, BAA01355, AAB35538, 1904153C, 1808265B, 1808265A, CAA36866, CAA36869, CAA36868, CAA36867, CAA36776, and AAA99436. Further, examples of nucleic acid molecules encoding MurG proteins have been deposited in NCBI, Genbank, and have Accession Nos. AL162758, AE002281, D90917, AF110367, AL139077, AJ242646, AE000520, AE000511, LA2023, U00096, NC-000922, AE000783, AE000657, AE001348, AF099188, AR048673, AR048672, AF179611, AL022602, AL109663, X55034, AE000621, D10602, AE001670, X64259, Y13922, U10879, AE001535, AF068902, AJ235271, AE000118, AE001227, AE001176, U94707, Z95388, U32793, AE000727, D84504, Z99111, D10483, X52644, X52540, and L24773. These sequences are known and are publicly available. Further, as additional genomes and genes are sequenced, more MurG encoding nucleotide sequences will become available, and can be used in the present invention.

In specific embodiments of the invention, the protein sequence of E. coli MurG was reported in 1990 (Ikeda et al. Nucleic Acids Res. 1990, 19:4014; and Mengin-Lecreuix, D. et al., Nucleic Acids Res. 1990, 18:2810.). E. coli genomic DNA can be purified from E. coli or purchased from ATCC, or the gene for E. coli MurG is cloned into a plasmid can be obtained from numerous sources. Primers were designed to the portions of the gene corresponding to the N and C termini of the protein. The primers also encoded restriction enzyme sites outside the protein coding region. The gene sequence was amplified; the corresponding double stranded nucleic acid molecule was cut with appropriate restriction enzymes for cloning into a commercially available expression vector (pET expression vectors available from Novagen provide for numerous variations of MurG protein—wild-type or fusion proteins or proteins with affinity tags at N or C terminus. We have worked with several constructs but found that MurG with a His-tag at C-terminus crystallized best; the protein sequence contained an extra methionine at N-terminus and eight extra residues at C terminus, six of which were histidines. The vector used was pET21b. (as described in Ha et al. J. Am. Chem. Soc. 121, (1999) 8415-8426 hereby incorporated by reference in its entirety).

A recombinant vector of the present invention can be either RNA (probably not) or DNA, and typically includes, but is not limited to, a virus or plasmid. Any recombinant vector and host cell that provides for expression of a MurG protein encoding mucleic acid sequence can be used in the present invention to express MurG protein for crystallization. Preferred vectors are engineered for high level expression in E. coli such as, but not limited to, pET vectors. We have found that over-expression of MurG from either E. coli or E. faecalis in E. coli cells is not toxic and, thus, this approach will work for other MurG proteins.

As used herein, an expression vector is a DNA vector that is capable of transforming a host cell and of affecting expression of a specified nucleic acid molecule. Expression vectors of the present invention include any vectors that function (i.e., direct gene expression) in recombinant cells of the present invention, including bacterial, fungal, and other microorganisms cells. Preferred expression vectors of the present invention direct expression in bacterial cells from a plasmid. A preferred recombinant molecule of the present invention comprises pET21b with E. coli MurG gene cloned into the Nde 1 and Xho 1 sites.

An expression vector of the present invention can be transformed into any suitable host cell to form a recombinant cell. A suitable host cell includes any cell capable of expressing a nucleic acid molecule inserted into the expression vector. For example, a procaryotic expression vector can be transformed into a bacterial host cell. If the expression vector contains a T7 promoter then a source of T7 RNA polymerase must be provided to induce expression. Some host cells contain the T7 RNA polymerase gene in a repressed state. Expression of T7 RNA polymerase can be induced with a chemical signal such as IPTG or heat. Alternatively, a source of T7 RNA polymerase can be introduced at the appropriate time by infection with a phage containing a copy of T7 RNA polymerase. A wide range of hosts strains can be infected with a suitable phage. Some host strains have been engineered to contain inducible copies of T7 RNA polymerase gene. Such host strains include BL21(DE3) and derivatives thereof. A preferred host strain of the present invention is BL21(DE3)pLysS or BL21(DE3)pLysE, which are commercially available from Novagen and can be readily transformed with a DNA plasmid vector containing a MurG gene under the control of the 17 promoter. As already stated above, a preferred vector is a pET vector, preferably containing a restriction enzyme site permitting cloning of the gene as a fusion containing a C-terminal his tag.

In a preferred embodiment, one method to isolate MurG protein useful for producing MurG crystals includes recovery of MurG protein having a C-terminal LEHHHHHH (His tag) sequence purified as described in Ha et al. (1999, J. Amer. Chem. Soc. 121:8415-8426). One of skill in the art is able to modify this procedure in order to purify other proteins can be produced as C-terminal histadine (his) tags. The purification conditions for specific MurG proteins will vary depending upon the particular characteristics of the proteins such as their isoelectric point, molecular weight, etc. It is known that the isoelectric points of different MurG homologues vary a bit, although they are generally relatively high. Also, some MurG homologues may be more hydrophobic than others, which will mean differences in amount of detergent necessary for purification. It is likely that all the MurG homologues can be purified over nickel affinity columns using the C-terminal his-tag as a handle. Those skilled in the art of protein purification will know how to modify purification parameters depending upon the protein characteristics, in order to purify the protein for crystallization.

Structure of MurG Protein

One embodiment of the present invention includes a model of a MurG protein, in which the model represents a three-dimensional structure of a MurG protein. Another embodiment of the present invention includes the three-dimensional structure of a MurG protein. A three-dimensional structure of a MurG protein encompassed by the present invention substantially conforms with the atomic coordinates represented in Table 1. According to the present invention, the use of the term “substantially conforms” refers to at least a portion of a three-dimensional structure of a MurG protein which is sufficiently spatially similar to at least a portion of a specified three-dimensional configuration of a particular set of atomic coordinates (e.g., those represented by Table 1) to allow the three-dimensional structure of another MurG protein to be modeled or calculated using the particular set of atomic coordinates defining the three-dimensional configuration of the MurG protein. For example, but not meant to be a limitation, homology modeling can be done using the linear sequence of a different MurG and E. coli coordinates; molecular replacement can allow the solution of a different MurG structure using the E. coli MurG coordinates and experimental data such as x-ray diffraction pattern from a different MurG crystal. According to the present invention, a three-dimensional structure of a given portion or chain of a first MurG protein can substantially conform to at least a portion of the atomic coordinates which represent a three-dimensional configuration of a second MurG.

More particularly, a structure that substantially conforms to a given set of atomic coordinates is a structure wherein at least about 50% of such structure has an average root-mean-square deviation (RMSD) of less than about 2.5 Å for the α-carbon or C-alpha backbone atoms in secondary structure elements in each domain, and more preferably, less than about 2.0 Å for the C-alpha backbone atoms in secondary structure elements in each domain, and, in increasing preference, less than about 1.5 Å, less than about 1.0 Å, less than about 0.7 Å, and more preferably, less than about 0.5 Å for the C-alpha backbone atoms in secondary structure elements in each domain. In a more preferred embodiment, a structure that substantially conforms to a given set of atomic coordinates is a structure wherein at least about 75% of such structure has the recited average root-mean-square deviation (RMSD) value, and more preferably, at least about 90% of such structure has the recited average RMSD value, and most preferably, about 100% of such structure has the recited average RMSD value.

In an even more preferred embodiment, the above definition of “substantially conforms” can be extended to include atoms of amino acid side chains. As used herein, the phrase “common amino acid side chains” refers to amino acid side chains that are common to both the structure which substantially conforms to a given set of atomic coordinates and the structure that is actually represented by such atomic coordinates. Preferably, a three-dimensional structure that substantially conforms to a given set of atomic coordinates is a structure wherein at least about 50% of the common amino acid side chains have an average RMSD value of less than about 1.5 Å, and more preferably, less than about 1.3 Å, and in increasing preference, less than about 1.0 Å, less than about 0.7 Å, and most preferably, less than about 0.3 Å.

In a more preferred embodiment, a structure that substantially conforms to a given set of atomic coordinates is a structure wherein at least about 75% of the common amino acid side chains have the recited average RMSD value, and more preferably, at least about 90% of the common amino acid side chains have the recited average RMSD value, and most preferably, about 100% of the common amino acid side chains have the recited average RMSD value.

In more preferred embodiments of the present invention, a large number of different “rotamers” or “rotational isomers” of the MurG protein are encompassed by three-dimensional structures of the invention in which the amino acid side chains are at a variety of positions in crystalline forms of the protein or for the protein in solution. Different rotamers refer to molecules of identical configuration may be distinguished as having different conformations after rotation about the various molecular bonds. Therefore, while the same or similar amino acids may be present, the exact location will vary depending upon the freedom of rotation of the bonds due to hydrogen bonding, and other molecular forces.

Structure of the α-Carbon Backbone OF MurG and the α-Carbon Backbone and Conserved Amino Acid Residues

The present invention includes the three-dimensional structure of the α-carbon or C-alpha backbone of a MurG protein, in particular the E. Coli MurG protein. A three-dimensional structure of the C-alpha backbone of the MurG protein encompassed by the present invention substantially conforms with the atomic coordinates represented in Table 2.

More particularly, a structure that substantially conforms to a given set of atomic coordinates is a structure wherein at least about 50% of such structure has an average root-mean-square deviation (RMSD) of less than about 2.5 Å for the C-alpha backbone atoms in secondary structure elements in each domain, and more preferably, less than about 2.0 Å for the C-alpha backbone atoms in secondary structure elements in each domain, and, in increasing preference, less than about 1.5 Å, less than about 1.0 Å, less than about 0.7 Å, and more preferably, less than about 0.5 Å for the C-alpha backbone atoms in secondary structure elements in each domain. In a more preferred embodiment, a structure that substantially conforms to a given set of atomic coordinates is a structure wherein at least about 75% of such structure has the recited average root-mean-square deviation (RMSD) value, and more preferably, at least about 90% of such structure has the recited average RMSD value, and most preferably, about 100% of such structure has the recited average RMSD value. The C-alpha backbone of MurG proteins is expected to be more conserved than the location of the particular amino acid residue side chains.

The present invention also includes the three-dimensional structure of the α-carbon or C-alpha backbone and conserved or invariant amino acid residue side chains of a MurG protein, in particular the E. coli MurG protein. A three-dimensional structure of the C-alpha backbone and conserved amino acid residues of the MurG protein encompassed by the present invention substantially conforms with the atomic coordinates represented in Table 3. The conserved amino acids are highlighted in blue in FIG. 3 a and include G14, G15, G18, H19, G104, H124, E125, G190, G191, S192, G194, A195, R261, G263, A264, E269, P281, Q289, N292 and A293 (as numbered in the E. Coli MurG sequence set forth in FIG. 3 a).

More particularly, a structure that substantially conforms to a given set of atomic coordinates is a structure wherein at least about 50% of such structure has an average root-mean-square deviation (RMSD) of less than about 2.5 Å, for the C-alpha backbone and conserved amino acid residue atoms in secondary structure elements in each domain, and more preferably, less than about 2.0 Å for the backbone atoms in secondary structure elements in each domain, and, in increasing preference, less than about 1.5 Å, less than about 1.0 Å, less than about 0.7 Å, and more preferably, less than about 0.5 Å for the backbone atoms in secondary structure elements in each domain. In a more preferred embodiment, a structure that substantially conforms to a given set of atomic coordinates is a structure wherein at least about 75% of such structure has the recited average rootmean-square deviation (RMSD) value, and more preferably, at least about 90% of such structure has the recited average RMSD value, and most preferably, about 100% of such structure has the recited average RMSD value.

Structure of the Donor Nucleotide Binding Site of MurG Proteins

An embodiment of the present invention includes the three-dimensional structure of a donor nucleotide binding site of a MurG protein, in particular an E. coli MurG protein. A more preferred embodiment of the present invention includes a three-dimensional structure of a donor nucleotide binding site of a MurG protein wherein the three-dimensional structure of the donor nucleotide binding site substantially conforms to the atomic coordinates in Table 4. In a preferred embodiment, the donor nucleotide binding site is a UDP-GlcNAc binding site of a MurG protein.

As described in Example 1, the donor nucleotide binding site is located in the C-terminal domain (see FIG. 4 a). This binding site is based on the comparison of β-glucosyltransferase (BGT) and E. coli MurG and based on experiments done in our laboratory showing that the isolated C domain binds to a UDP-hexose column (See Example 1). The atomic coordinates of Table 4 set forth the donor nucleotide binding site three-dimensional structure without a donor nucleotide such as UDP-GlcNAc bound to the MurG protein.

According to the present invention, the use of the term “substantially conforms” refers to at least a portion of a three-dimensional structure of a donor nucleotide binding site of a MurG protein which is sufficiently spatially similar to at least a portion of a specified three-dimensional configuration of a particular set of atomic coordinates (e.g., those represented by Table 4) to allow the three-dimensional structure of the donor nucleotide binding domain to be modeled or calculated (i.e., by molecular replacement) using the particular set of atomic coordinates defining the three-dimensional configuration of the donor nucleotide binding site of a MurG protein. According to the present invention, a three-dimensional structure of a given donor nucleotide binding site of a first MurG protein can substantially conform to at least a portion of the atomic coordinates which represent a three-dimensional configuration of a second MurG. Since the atomic coordinates of Table 4 were obtained from the E. coli MurG crystal protein without a donor nucleotide bound, there will be some variation from the atomic coordinates of the donor nucleotide binding site when a nucleotide is bound vs. unbound. Therefore, a structure “substantially conforming” to that represented by the atomic coordinates in Table 4, will include a structure obtained from co-crytallization of the protein with a donor nucleotide.

More particularly, a structure that substantially conforms to a given set of atomic coordinates is a structure wherein at least about 50% of such structure has an average root-mean-square deviation (RMSD) of less than about 1.5 Å for the C-alpha backbone atoms in secondary structure elements in each domain, and more preferably, less than about 1.3 Å for the C-alpha backbone atoms in secondary structure elements in each domain, and, in increasing preference, less than about 1.0 Å, less than about 0.7 Å, and more preferably less than about 0.5 Å for the C-alpha backbone atoms in secondary structure elements in each domain. In a more preferred embodiment, a structure that substantially conforms to a given set of atomic coordinates is a structure wherein at least about 75% of such structure has the recited average root-mean-square deviation (RMSD) value, and more preferably, at least about 90% of such structure has the recited average RMSD value.

In an even more preferred embodiment, the above definition of “substantially conforms” can be extended to include atoms of the conserved or invariant amino acid side chains located within the binding site. As used herein, the phrase “conserved amino acid side chains” refers to amino acid side chains that are conserved between MurG proteins within the donor nucleotide binding site. The conserved amino acid residues of the donor nucleotide binding site have been identified as I125, R261, G263, A264, E269, P281, Q289, N292 and A293 (as numbered in the E. coli MurG sequence set forth in FIG. 3 a) and the G loop found between residues numbered 190-195 having residues G190, G191, S192, G194, and A195. Some or all of these conserved residues are necessary for binding the nucleotide donor.

Preferably, a three-dimensional structure that substantially conforms to a given set of atomic coordinates is a structure wherein at least about 50% of the conserved amino acid side chains have an average RMSD value of less than about 1.5 Å, and more preferably, less than about 1.3 Å, and in increasing preference, less than about 1.0 Å, less than about 0.7 Å, and most preferably, less than about 0.3 Å. In a more preferred embodiment, a structure that substantially conforms to a given set of atomic coordinates is a structure wherein at least about 75% of the conserved amino acid side chains have the recited average RMSD value, and more preferably, at least about 90% of the conserved amino acid side chains have the recited average RMSD value, and most preferably, about 100% of the conserved amino acid side chains have the recited average RMSD value.

Structure of the Acceptor Binding Site of MurG Protein

An embodiment of the present invention includes the three-dimensional structure of an acceptor binding site of a MurG protein. A three-dimensional structure of a acceptor binding site of a MurG protein encompassed by the present invention substantially conforms with the atomic coordinates represented in Table 5. A more preferred embodiment of the present invention includes a three-dimensional structure of an acceptor binding site of a MurG protein wherein the three dimensional structure of the acceptor binding site substantially conforms to the atomic coordinates Table 5.

According to the present invention, the use of the term “acceptors” refers to Lipid I and analogues thereof. For the purposes of obtaining co-crystals containing acceptor analogues bound to the acceptor binding site better, the analogues need not be functional acceptors in a MurG assay. In particular embodiments of the present invention, the acceptor is selected from the group consisting of, but not limited to Lipid I, and analogs of Lipid I (see compounds described in Ha et al., J. Amer. Chem. Soc. 1999, vol. 121:8415-26, incorporated by herein by reference in its entirety).

As described in Example 1, the acceptor binding site is located in the N-terminal domain of a MurG protein (see FIGS. 3 a and 4 c). The acceptor binding site or domain is characterized by three highly conserved regions, twp of which are glycine-rich loops (also referred to as “G loops”) that face the cleft between the C-terminal and N-terminal domains. The conserved residues of the acceptor binding site comprise G14, G15, G18, H19, G104, H124, and E125 (as numbered in the E. coli MurG sequence set forth in FIG. 3 a) and two conserved G loop structures.

According to the present invention, the use of the term “substantially conforms” refers to at least a portion of a three-dimensional structure of an acceptor binding site of a MurG protein which is sufficiently spatially similar to at least a portion of a specified three-dimensional configuration of a particular set of atomic coordinates (e.g., those represented by Table 5) to allow the three-dimensional structure of the acceptor binding site to be modeled or calculated (i.e., by homology modeling) using the particular set of atomic coordinates defining the three-dimensional configuration of the acceptor binding site of a MurG protein. According to the present invention, a three-dimensional structure of a given acceptor binding site of a first MurG protein can substantially conform to at least a portion of the atomic coordinates which represent a three-dimensional configuration of a second MurG.

In an even more preferred embodiment, the above definition of “substantially conforms” can be extended to include atoms of the conserved amino acid side chains. As used herein, the phrase “conserved amino acid side chains” refers to the conserved or invariant amino acid side chains that are common to MurG proteins. Preferably, a three-dimensional structure that substantially conforms to a given set of atomic coordinates is a structure wherein at least about 50% of the conserved amino acid side chains have an average RMSD value of less than about 1.5 Å, and more preferably, less than about 1.3 Å, and in increasing preference, less than about 1.0 Å, less than about 0.7 Å, and most preferably, less than about 0.3 Å. In a more preferred embodiment, a structure that substantially conforms to a given set of atomic coordinates is a structure wherein at least about 75% of the conserved amino acid side chains have the recited average RMSD value, and more preferably, at least about 90% of the conserved amino acid side chains have the recited average RMSD value, and most preferably, about 100% of the conserved amino acid side chains have the recited average RMSD value.

Structure of a Membrane Association Site of MurG Protein

An embodiment of the present invention includes the three-dimensional structure of a membrane association site of a MurG protein. A three-dimensional structure of a membrane association site of a MurG protein encompassed by the present invention substantially conforms with the atomic coordinates represented in Table 6. A more preferred embodiment of the present invention includes a three-dimensional structure of an acceptor binding site of a MurG protein wherein the three-dimensional structure of the acceptor binding site substantially conforms to the atomic coordinates in Table 6.

According to the present invention, the use of the term “membrane association site” refers to the region of a MurG protein that associates with cytoplasmic surface of bacterial membranes where it performs the reaction of coupling a soluble donor sugar to the membrane anchored acceptor sugar, Lipid I. Analysis of the E. coli MurG protein structure shows a hydrophobic patch consisting of residues I75, L79, F82, W85, and W116 in the N-domain. The membrane association site is where the MurG protein associates with the bacterial membranes, and that it is target for inhibitors if we find that a) we can bind to it with another molecule; b) we can disrupt membrane association by binding to it; or c) disrupting membrane association inhibits activity.

As described in Example 1, the membrane association site is located in the N-terminal domain of a Mur protein (see FIG. 4 c). The location of the membrane association site is in close proximity to the acceptor binding site and membrane association in this patch would bring the two M-terminal G-loops close to the membrane surface where the diphosphate portion of the acceptor is located.

According to the present invention, the use of the term “substantially conforms” refers to at least a portion of a three-dimensional structure of a membrane association site of a MurG protein which is sufficiently spatially similar to at least a portion of a specified three-dimensional configuration of a particular set of atomic coordinates (e.g., those represented by Table 6) to allow the three-dimensional structure of the membrane association site to be modeled or calculated (i.e., by molecular replacement) using the particular set of atomic coordinates defining the three-dimensional configuration of the membrane association site of a MurG protein. According to the present invention, a three-dimensional structure of a given membrane association site of a first MurG protein can substantially conform to at least a portion of the atomic coordinates which represent a three-dimensional configuration of a second Mur).

More particularly, a structure that substantially conforms to a given set of atomic coordinates is a structure wherein at least about 50% of such structure has an average root-mean-square deviation (RMSD) of less than about 1.5 Å for the structural elements in the site, and more preferably, less than about 1.3 Å for the structure elements in each site, and, in increasing preference, less than about 1.0 Å, less than about 0.7 Å, less than about 0.5 Å, and more preferably, less than about 0.3 Å for the structural elements in each site. In a more preferred embodiment, a structure that substantially conforms to a given set of atomic coordinates is a structure wherein at least about 75% of such structure has the recited average root-mean-square deviation (RMSD) value, and more preferably, at least about 90% of such structure has the recited average RMSD value, and most preferably, about 100% of such structure has the recited average RMSD value.

In an even more preferred embodiment, the above definition of “substantially conforms” can be extended to include atoms of α-carbon backbone and conserved amino acid side chains. As used herein, the phrase “conserved amino acid side chains” refers to amino acid side chains that are conserved between MurG proteins. Preferably, a three-dimensional structure that substantially conforms to a given set of atomic coordinates is a structure wherein at least about 50% of the conserved α-carbon backbone and conserved amino acid side chains have an average RMSD value of less than about 1.5 Å, and more preferably, less than about 1.3 Å, and in increasing preference, less than about 1.0 Å, less than about 0.7 Å, and most preferably, less than about. 0.3 Å. In a more preferred embodiment, a structure that substantially conforms to a given set of atomic coordinates is a structure wherein at least about 75% of the α-carbon backbone and conserved amino acid side chains have the recited average RMSD value, and more preferably, at least about 90% of the α-carbon backbone and conserved acid side chains have the recited average RMSD value, and most preferably, about 100% of the α-carbon and conserved amino acid side chains have the recited average RMSD value.

Computer Readable Medium

Another embodiment of the present invention relates to a computer-readable medium encoded with a set three-dimensional coordinates selected from the group consisting of the three-dimensional coordinates represented in Table 1, the three-dimensional coordinates represented in Table 2, the three-dimensional coordinates represented in Table 3, the three-dimensional coordinates represented in Table 4, the three-dimensional coordinates represented in Table 5, or the three-dimensional coordinates represented in Table 6, wherein using a graphical display software program, the three-dimensional coordinates create an electronic file that can be visualized on a computer capable of representing said electronic file as a three-dimensional image. Preferably, the three-dimensional image is of a MurG protein, the α-carbon backbone of MurG, the α-carbon backbone and conserved amino acid residue sidechains of MurG, the donor nucleotide binding site of MurG, the acceptor binding site of MurG, or the membrane association site of MurG.

Yet another embodiment of the present invention relates to a computer-readable medium encoded with a set of three-dimensional coordinates of a three-dimensional structure which substantially conforms to the three-dimensional coordinates represented in Table 1, wherein using a graphical display software program, the three-dimensional coordinates create an electronic file that can be visualized on a computer capable of representing said electronic file as a three-dimensional image. In other embodiments, the present invention relates to a computer-readable medium encoded with a set of three-dimensional coordinates of a three-dimensional structure which substantially conforms to the three-dimensional coordinates represented in Table 2, Table 3, Table 4, Table 5 or Table 6, wherein using a graphical display software program, the three-dimensional coordinates create an electronic file that can be visualized on a computer capable of representing said electronic file as a three-dimensional image. Preferably, the three-dimensional image is of a MurG protein, the α-carbon backbone of MurG, the α-carbon backbone and conserved amino acid residue sidechains of MurG, the donor nucleotide binding site of MurG, the acceptor binding site of MurG, or the membrane association site of MurG.

Images

One embodiment of the present invention relates to a two dimensional image of an E. coli MurG protein including those illustrated in FIGS. 3-4. Most of these figures were drawn with the MOLSCRIPT program. Preferably, the two dimensional image is of a MurG protein, the α-carbon backbone of MurG, the α-carbon backbone and conserved amino acid residue sidechains of MurG, the donor nucleotide binding site of MurG, the acceptor binding site of MurG, or the membrane association site of MurG.

Another embodiment of the present invention includes a three-dimensional computer image of the three-dimensional structure of a MurG protein, preferably the E. coli MurG protein. Suitable structures of which to produce three-dimensional computer images are disclosed herein. Preferably, a computer image is created to a structure substantially conforming with the three-dimensional coordinates represented in Table 1.

Another embodiment of the present invention includes an image of an MurG protein that is generated when a set of three-dimensional coordinates comprising the three-dimensional coordinates represented in Table I are analyzed on a computer using a graphical display software program to create an electronic file of the image and visualizing the electronic file as a three-dimensional image. Suitable structures to image are disclosed herein. Preferably, the three-dimensional structures are of a MurG protein, the α-carbon backbone of MurG, the α-carbon backbone and conserved amino acid residue sidechains of MurG, the donor nucleotide binding site of MurG, the acceptor binding site of MurG, or the membrane association site of MurG. Most preferably, the MurG protein is the E. coli MurG protein described herein. A computer image of the present invention can. be produced using any suitable software program, including, but not limited to, MOLSCRIPT 2.0 (Avatar Software AB, Helenebrgsgatan 21 C, SE-11713, Stockholm, Sweden), the graphical display program 0 (Jones et al., Acta Crystallography, vol. A47, p. 110, 1991), or the graphical display program GRASP. Suitable computer hardware useful for producing an image of the present invention are known to those of skill in the art. Preferred computer hardware includes a Silicon Graphics Workstation.

Models of MurG Proteins and Binding Sites

According to the present invention, a three-dimensional structure of the E. coli MurG protein and its binding sites of the present invention can be used to derive a model of the three-dimensional structure of another MurG protein and its binding sites (i.e., a structure to be modeled). As used herein, a “structure” of a protein refers to the components and the manner of arrangement of the components to constitute a protein or binding site. Also, as used herein, the term “model” refers to a representation of a tangible medium of the three-dimensional structure of a protein, polypeptide or peptide, or binding site of a protein. For example, a model can be a representation of the three-dimensional structure in a electronic file, on a computer screen, on a piece of paper (i.e., on a two dimensional medium), and/or as a ball-and-stick figure. Physical three-dimensional models are tangible and include, but are not limited to, stick models and space-filling models. The phrase “imaging the model on a computer screen” refers to the ability to express (or represent) and manipulate the model on a computer screen using appropriate computer hardware and software technology known to those skilled in the art. Such technology is available from a variety of sources including, for example, Evans and Sutherland, Salt Lake City, Utah, and Biosym Technologies, San Diego, Calif. The phrase “providing a picture of the model” refers to the ability to generate a “hard copy” of the model. Computer screen images and pictures of the model can be visualized in a number of formats including space-filling representations, α-carbon traces, ribbon diagrams and electron density maps.

Suitable target MurG proteins and their associated binding sites to model using a method of the present invention include any MurG protein and binding sites that are at least in part structurally related to the E. coli MurG protein or its binding sites. A preferred target MurG structure that is at least in part structurally related includes a target MurG structure having an amino acid sequence that is at least about 25%, preferably at least about 30%, more preferably at least about 36%, more preferably at least about 40%, even more preferably at least about 50%, more preferably at least about 60%, more preferably at least about 70%, more preferably at least about 80%, and more preferably at least about 90% identical to an amino acid sequence of the E. coli MurG protein, across the full-length of the target MurG structure sequence when using, for example, a sequence alignment program such as DNAsiS™ program (available from Hitachi Software, San Bruno, Calif.) or the MacVector™ program (available from the Eastman Kodak Company, New Haven, Conn.) or the GCγ™ program (available from the “GCγ”, University of Wisconsin, Madison, Wis.), such alignment being performed for example, using the standard default values accompanying such alignment programs.

Preferred MurG proteins and their binding sites are set forth in the amino acid sequences of MurG proteins as deposited in the NCBI database and are identified with Accession Nos. CAB51993, A71316, E70579, C71699, F70195, A43727, JC1275, BVECMG, CEECAM, 083535, Q9ZK59, CAB85280, AAF39020, BAA18775, AAD26629, CAB73295, P37585, Q9ZHA9, Q9ZHDC0, Q9ZBA5, Q9X4H4, Q9WY74, P74657, O06224, Q9Z702, O84766, O69552, O67238, O51708, O25770, O07670, O07109, P45065, CAB66324, AAC68356, AAF06830, P18579, P17443, P17952, P16457, P07862, AAE23178, AAD53936, CAA18668, CAA38869, CAA38868, CAA38867, CAA38866, AAD08196, BAA01453, BAA01455, BAA01454, AAD19042, CAA45558, CAA74235, AAD10537, AAD06652, AAC95450, CAA14869, AAC73201, AAC65509, AAC67113, AAC45636, CAB08640, AAC22793, AAC07193, BAA24357, CAB13395, BAA01355, AAB35538, 1904153C, 1808265B, 1808265A, CAA36866, CAA36869, CAA36868, CAA36867, CAA36776, and AAA99436. The amino acid sequences are publicly available.

A variety of MurG proteins from numerous organisms can be used to prepare models of MurG proteins and binding sites, including but not limited to, microorganisms such as bacteria, higher-order bacteria, thermal stable bacteria, spirochetes, small pathogenic organisms, fungi, protozoa, cyanobacteria, and trypanosomes. More particularly, bacteria such as but not limited to, Escherichia coli, Bacillus subtilis, Aquefex aeolicus, Borrelia burgdorferi, Chlamydia pneumoniae, Chlamydia trachomatis, Enterococcus faecais, Enterococcus hirae, Haemophilus influenzae, Helicobacter pyloir J99, Helicobacter pylori, Mycobacterium tuberculosis, Porphyromonas gingivalis, Rickettsia prowazekii, Streptomyces coelicolor, Streptomyces collinus, Streptococcus pneumoniae, Synechocystis sp. (strain PCC6803), Thermotoga maritime, and Treponema pallidum. It is noted that nucleotide and amino acid sequences for many of the above identified organisms are known and publicly available.

Preferred target MurG proteins and binding site structures to model also include, but are not limited to, derivatives of MurG proteins, such as a MurG protein having one or more amino acid residues substituted, deleted or added (referred to herein as MurG mutants), or proteins encoded by natural variants of a nucleic acid molecule encoding a MurG.

In another embodiment of the invention, the process of building a homology model for a protein is divided into the following steps:

-   -   (1) Determine which proteins are related to the model protein;     -   (2) Determine structurally conserved regions (SCRs);     -   (3) Align the amino acid sequence of the unknown protein with         those of the reference protein(s) within the SCRs;     -   (4) Assign coordinates in the conserved regions;     -   (5) Predict conformations for the rest of the peptide chain,         including loops between the SCRs and possibly the N- and         C-termini;     -   (6) Search for the optimum side chain conformations for residues         that differ from those in the reference proteins; and     -   (7) Use energy minimization and molecular dynamics to refine the         molecular structure so that steric strain introduced during the         model-building process can be relieved.

Published sequences are readily available through on-line databases on the Internet, such as SwissProt (http://www.expasy.ch/sprot/sprot-top.html). MurG specific and related sequences are obtained for use for building homology models by text-based or sequence similarity searching. SCRs for MurG is the entire protein, considering the E. coli MurG crystal structure is the only similar sequence with structural data. Alignment of the sequences using an appropriate alignment program and algorithm, such as Clustal W, allows appropriate assignment of the E. coli protein coordinates to a MurG sequence of unknown structure. The Modeler program performs the conformational predictions for the peptide chain and side chains. Dynamics and minimization using an appropriate program and algorithm, such as Discover.

Modeler Description:

Modeler is an automated homology-modeling scheme designed to find the most probable three-dimensional structure of a protein, given its amino acid sequence and its alignment with related structures. It derives 3D protein models without the time consuming separate stages of core region identification and loop region building or searching that is inherent to manual homology modeling schemes. The related or reference protein structures are used to derive spatial restraints expressed as probability density functions (PDFs) for each of the restrained features of the model. As an example, the main chain conformation of a given residue in the model will be described by restraints that depend upon the residue type, the main chain conformation of equivalent residues in the reference proteins and the local sequence similarity. The probability distribution functions that are used in restraining the model structure are derived from correlations between structural features in a database of families of homologous proteins aligned on the basis of their 3D structure. These functions are used to restrain C—C distances, main chain N—O distances, main chain and side chain dihedral angles, etc. The individual restraints are assembled into a single molecular probability density function (MPDF). The three-dimensional protein model is then obtained by an optimization of this MPDF. The optimization procedure itself consists of a variable target function method (Braun and Go, 1985) with conjugate gradient minimization scheme followed by an optional restrained simulated annealing molecular dynamics scheme.

While several reference structures are used in the traditional homology model building process, only one set of coordinates can be used in any one peptide segment. Modeler is able to simultaneously incorporate structural data from one or more reference proteins. Structural features in the reference proteins are used to derive spatial restraints which in turn are used to generate model protein structures using conjugate gradient and simulated annealing optimization procedures.

Clustal W description:

Clustal W aligns multiple sequences using a progressive pairwise alignment algorithm. It first generates all possible pairwise alignments for a list of sequences and then builds the guide tree based on their pairwise sequence identity, aligning the sequences following the order of the guide tree.

Several unique features in Clustal W improve the sensitivity of the alignment of divergent protein sequences (Thompson et al, 1994a).

(1) Individual weights are assigned to each sequence in a partial alignment in order to downweight near-duplicate sequences and upweight the most divergent ones.

(2) Amino acid substitution matrices are varied at different alignment stages according to the divergence of the sequences to be aligned.

(3) Residue-specific gap penalties and locally reduced gap penalties in hydrophilic regions encourage new gaps in potential loop regions rather than regular secondary structure.

(4) Positions in early alignments, where gaps have been opened, receive locally reduced gap penalties to encourage the opening of new gaps at these positions.

Discover Description:

The Discover program performs energy minimization, template forcing, torsion forcing, and dynamic trajectories and calculates properties such as interaction energies, derivatives, mean square displacements, and vibrational frequencies. It provides tools for performing simulations under various conditions including constant temperature, constant pressure, constant stress, periodic boundaries, and fixed and restrained atoms.

Homology modeling methods are known to those skilled in the art and are described in the following homology references:

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The Modeler Program is known to those skilled in the art and is discussed in the following references:

-   Bernstein, F. C.; T. F. Koetzle, G. J. B. Williams, E. F. Meyer     Jr, M. D. Brice, J. R. Rodgers, O. Kennard, T. Schimanouchi, M.     Tasumi, “The protein data bank: A computer based archival file for     macromolecular structures,” J. Mol. Biol. 112, 535-542 (1977). -   Blundell, T. L.; B. L. Sibanda; M. J. E. Sternberg; J. M. Thornton     “Knowledge-based prediction of protein structures and the design of     novel molecules” Nature (London) 326 347-352 (1987). -   Blundell, T. L.; D. Carney; S. Gardner; F. Hayes; B. Howlin: T.     Hubbard; J. Overinton; D. A. Singh; B. L. Sibanda; M. Sutcliff     “Knowledge-based protein modelling and design” Eur. J. Biochem.     172-513 (1988) -   Browne, W. J.; A. C. T. North; D. C. Phillips; K. Brew; T. C.     Vanaman; R. C. Hill “A possible three-dimensional structure of     bovine-lactalbumin based on that of hen's eggwhite lysozyme” J. Mol.     Biol. 42 65-86 (1969). -   Braun, W. and N. Go “Calculation of protein conformations by     proton-proton distance constraints: A new efficient algorithm” J.     Mol. Biol. 186, 611-626 (1985). -   Brooks, B. R.; R. E. Bruccoleri, B. D. Olafson, D. J. States, S.     Swarninathan, M. Karplus, J. Comp. Chem. 4, 187 (1983) -   Greer, J. “Model for haptoglobin heavy chain based upon structural     homology” Proc. Nat. Acad. Se. U.S.A. 77 3393 (1980). -   Greer, J. “Comparative model-building of the mammalian serine     proteases” J. Mol. Biol. 153 1027-1042 (1981). -   Greer, J. “Model structure for the Inflammatory Protein C5a” Science     228 1055 (1985). -   Matsumoto, R., A. ali, N. Ghildyal, M. Karplus, R. L. Stevens     “Packaging of proteases and proteoglycans in the granules of mast     cells and other hematopoietic cells” J. Biol. Chem, 270, 19524-19531     (1995). -   Melo, F. & Feytnans, E. “Novel knowledge-based mean force potential     at the atomic level” J. Mol. Biol. 267, 207-222 (1997) -   Nilsson, L.; M. Karplus, J. Comp. Chem., 7, 591 (1986). -   Ponder, Richards, J. Mol. Biol. 194 775-791 (1987). -   Sali, A. “Modeling mutations and homologous proteins,” Curr. Opin.     Biotech., 6 437-451 (1995a). -   Sali, A. “Protein modeling by satisfaction of spatial restraints”     Molecular Medicine Today, 1 270-277 (1995b). -   Sali, A.; T. L. Blundell, “Definition of general topological     equivalence in protein structures: A procedure involving comparison     of properties and relationships through simulated annealing and     dynamic programming,” J. Mol. Biol., 212 403-428 (1990). -   Sali, A.; T. L. Blundell, “Comparative protein modeling by     satisfaction of spatial restraints,” Mol. Biol., 234 779-815     (1993a). -   Sali, A.; R. Matsumoto, H. P. McNeil, M. Karplus, R. L. Stevens,     “Three-dimensional models of four mouse mast cell chymases.     Identification of proteoglycan-binding regions and protease-specific     antigenic epitopes,” J. Biol. Chem., 268 9023-9034 (1993b). -   Sali, A.; J. P. Overington, “Derivation of rules for comparative     protein modeling from a database of protein structure     alignments,”Protein Sci., 31, 582-1596 (1994). -   Sali, A.; L. Pottertone, F. Yuan, H. van Vlijmen and M. Karplus     “Evaluation of comparative protein modeling by MODELLER” Proteins     23, 318-326 (1995). -   Shotton, D. M.; H. C. Watson “Three-dimensional STructure of     Tosyl-elastase” Nature 225 811 (1970).

The CFF Force Field is known to those skilled in the art and is discussed in the following references:

-   Baldridge, K.; Fine, R.; Hagler, A. J. Comp. Chem. 15, 1217-1227     (1994). -   Dinur, U.; Hagler, A. T. J. Amer. Chem. Soc. 111, 5149-5151 (1989). -   Dinur, U.; Hagler, A. T. In Reviews in Computational Chemistry, Vol.     2, K. B. Lipkowitz; D. B. Boyd, Eds., VCH Publishers: New York,     99-164 (1991). -   Francl, M. M.; Pietro, W. J.; Hehre, W. J.; Binkley, J. S.;     Gordon, M. S.; DeFrees, D. J.; Pople, J. A. J. Chem. Phys. 77,     3654-3665 (1982). -   Hagler, A. T.; Huler, E.; Lifson, S. J. Amer. Chem. Soc. 96,     5319-5327(1974). -   Hagler, A. T.; Lifson, S.; Dauber, P. J. Amer. Chem. Soc. 101,     5122-5130 (1979a). -   Hagler, A. T.; Dauber, P.; Lifson, S. J. Amer. Chem. Soc.—101,     5131-5141 (1979b). -   Hariharan, P. C.; Pople, J. A. Theor. Chim. Acta 28, 213-222 (1973). -   Hassan, M.; Nguyen, D. T.; Li, Z.; Hwang, M.-J.; Kitson, D. H.;     Hagler, A. T. (in preparation). -   Hwang, M.-J.; Stockfisch, T. P.; Hagler, A. T. J. Amer. Chem. Soc.     116, 2515-2525 (1994). -   Kurihara, H.; Nguyen, D. T.; Hassan, M.; Hagler, A. T. (in     preparation). -   Maple, J. R.; Hwang, M-J.; Stockfisch, T. P.; Dinur, U.; Waldman,     M.; Ewig, C. S.; Hagler, A. T. J. Comp. Chem. 15, 162-182 (1994). -   Michalska, D.; Schaad, L. J.; Carsky, P.; Hess, Jr., B. A.;     Ewig, C. S. J. Comp. Chem., 9, 495(1988). -   Waldman, M.; Hagler, A. T. J. Comp. Chem. 14, 1077-1084 (1993).

All the references cited above are incorporated by reference in the entireties.

Structure Based Drug Design

The present invention relates to the use of the crystal structure of the E. coli MurG protein represented by the atomic coordinates in Table 1 to make models of MurG proteins and binding sites thereof. The present invention also relates to the use of the crystal structure, α-carbon backbone, α-carbon backbone plus conserved amino acid residue side chains or binding sites of the E. coli MurG protein to construct models of these structures in other MurG proteins.

For the first time, the present invention permits the use of molecular design techniques to design, select and synthesize chemical entities and compounds, including inhibitory compounds, capable of binding to the active site or accessory binding site of MurG, in whole or in part.

On approach enabled by this invention, is to use the structure coordinates of MurG to design compounds that bind to the enzyme and alter the physical properties of the compounds in different ways, e.g., solubility. For example, this invention enables the design of compounds that act as inhibitors of the MurG enzyme by binding to, all or a portion of, the active site of MurG.

A second design approach is to probe a MurG crystal with molecules composed of a variety of different chemical entities to determine optimal sites for interaction between candidate MurG inhibitors and the enzyme. For example, high resolution X-ray diffraction data collected from crystals saturated with solvent allows the determination of where each type of solvent molecule sticks. Small molecules that bind tightly to those sites can then be designed and synthesized and tested for their MurG inhibitor activity. Travis, J., Science, 262, p. 1374 (1993).

This invention also enables the development of compounds that can isomerize to short-lived reaction intermediates in the chemical reaction of a substrate or other compound that binds to MurG, with MurG. Thus, the time-dependent analysis of structural changes in MurG during its interaction with other molecules is enabled. The reaction intermediates of MurG can also be deduced from the reaction product in co-complex with MurG. Such information is useful to design improved analogues of known MurG inhibitors or to design novel classes of inhibitors based on the reaction intermediates of the MurG enzyme and MurG-inhibitor co-complex. This provides a novel route for designing MurG inhibitors with both high specificity and stability.

Another approach made possible and enabled by this invention, is to screen computationally small molecule data bases for chemical entities or compounds that can bind in whole, or in part, to the MurG enzyme. In this screening, the quality of fit of such entities or compounds to the binding site may be judged either by shape complementarity or by estimated interaction energy. Meng, E. C. et al., J. Coma. Chem., 13, pp. 505-524 (1992).

Because MurG may crystallize in more than one crystal form, the structure coordinates of MurG, or portions thereof, as provided by this invention are particularly useful to solve the structure of those other crystal forms of MurG. They may also be used to solve the structure of MurG mutants, MurG co-complexes, or of the crystalline form of any other protein with significant amino acid sequence homology to any functional domain of MurG.

One method that may be employed for this purpose is molecular replacement. In this method, the unknown crystal structure, whether it is another crystal form of MurG a MurG mutant, or a MurG co-complex, or the crystal of some other protein with significant amino acid sequence homology to any functional domain of MurG, may be determined using the MurG structure coordinates of this invention as provided in Tables 1-6. This method will provide an accurate structural form for the unknown crystal more quickly and efficiently than attempting to determine such information ab initio.

In addition, in accordance with this invention, MurG mutants may be crystallized in co-complex with known MurG inhibitors. The crystal structures of a series of such complexes may then be solved by molecular replacement and compared with that of wild-type MurG. Potential sites for modification within the various binding sites of the enzyme may thus be identified. This information/provides an additional tool for determining the most efficient binding interactions, for example, increased hydrophobic interactions, between MurG and a chemical entity or compound.

All of the complexes referred to above may be studied using well-known X-ray diffraction techniques and may be refined versus 2-3 .ANG. resolution X-ray date to an R value of about 0.20 or less using computer software, such as X-PLOR (Yale University, .COPYRGT.1992, distributed by Molecular Simulations, Inc.). See, e.g., Blundel & Johnson, supra; Methods in Enzvmoloav, vol. 114 & 115, H. W. Wyckoff et al., eds., Academic Press (1985). This information may thus be used to design, synthezie and optimize novel classes of MurG inhibitors.

The structure coordinates of MurG mutants provided in this invention also facilitate the identification of related proteins or enzymes analogous to MurG in function, structure or both, thereby further leading to novel therapeutic modes for treating or preventing UDP-glycosyltaansferase mediated diseases.

The design of compounds that bind to or inhibit MurG according to this invention generally involves consideration of two factors. First, the compound must be capable of physically and structurally associating with MurG. Non-covalent molecular interactions important in the association of MurG with its substrate include hydrogen bonding, van der Waals and hydrophobic interactions.

Second, the compound must be able to assume a conformation that allows it to associate with MurG. Although certain portions of the compound will not directly participate in this association with MurG, those portions may still influence the overall conformation of the molecule. This, in turn, may have a significant impact on potency. Such conformational requirements include the overall three-dimensional structure and orientation of the chemical entity or compound in relation to all or a portion of the binding site, e.g., active site or accessory binding site of MurG, or the spacing between functional groups of a compound comprising several chemical entities that directly interact with MurG.

The potential inhibitory or binding effect of a chemical compound on MurG may be analyzed prior to its actual synthesis and testing by the use of computer modelling techniques. If the theoretical structure of the given compound suggests insufficient interaction and association between it and MurG, synthesis and testing of the compound is obviated. However, if computer modelling indicates a strong interaction, the molecule may then be synthesized and tested for its ability to bind to MurG and inhibit using the assay of Walker et al. patents (cited supra). In this manner, synthesis of inoperative compounds may be avoided.

An inhibitory or other binding compound of MurG may be computationally evaluated and designed by means of a series of steps in which chemical entities or fragments are screened and selected for their ability to associate with the individual binding pockets or other areas of MurG.

One skilled in the art may use one of several methods to screen chemical entities or fragments for their ability to associate with MurG and more particularly with the individual binding pockets of the MurG donor nucleotide binding site, acceptor binding site or membrane association site. This process may begin by visual inspection of, for example, the binding sites on the computer screen based on the MurG coordinates in Tables 1-6. Selected fragments or chemical entities may then be positioned in a variety of orientations, or docked, within an individual binding pocket of MurG as defined supra. Docking may be accomplished using software such as Quanta and Sybyl, followed by energy minimization and molecular dynamics with standard molecular mechanics forcefields, such as CHARMM and AMBER.

Specialized computer programs may also assist in the process of selecting fragments or chemical entities, including but not limited to:

-   -   1. GRID (Goodford, P. J., “A Computational Procedure for         Determining Energetically Favorable Binding Sites on         Biologically Important Macromolecules” J. Med. Chem., 28, pp.         849-857 (1985)). GRID is available &orn Oxford University,         Oxford, UK.     -   2. MCSS (Miranker, A. and M. Karplus, “Functionality Maps of         Binding Sites: A Multiple Copy Simultaneous Search Method.”         Proteins: Structure, Function and Genetics, 11, pp. 29-34         (1991)). MCSS is available from Molecular Simulations,         Burlington, Mass.     -   3. AUTODOCK (Goodsell, D. S. and A. J. Olsen, “Automated Docking         of Substrates to Proteins by Simulated Annealing” Proteins:         Structure. Function, and Genetics, 8, pp. 195-202 (1990))         (AUTODOCK is available from Scripps Research Institute, La         Jolla, Calif.).     -   4. DOCK (Kuntz, I. D. et al., “A Geometric Approach to         Macromolecule-Ligand Interactions” J. Mol. Biol., 161, pp.         269-288 (1982)). DOCK is available from University of         California, San Francisco, Calif.

Once suitable chemical entities or fragments have been selected, they can bc assembled into a single compound or inhibitor. Assembly may be proceeded by visual inspection of the relationship of the fragments to each other on the three-dimensional image displayed on a computer screen in relation to the structure coordinates of MurG. This would be followed by manual model building using software such as Quanta or Sybyl.

Useful programs to aid one of skill in the art in connecting the individual chemical entities or fragments include, but are not limited to:

-   -   1. CAVEAT (Bartlett, P. A. et al, “CAVEAT: A Program to         Facilitate the Structure-Derived Design of Biologically Active         Molecules”. In Molecular Recognition in Chemical and Biological         Problems”, Special Pub., Royal Chem. Soc., 78, pp. 182-196         (1989)). CAVEAT is available from the University of California,         Berkeley, Calif.     -   2. 3D Database systems such as MACCS-3D (MDL Information         Systems, San Leandro, Calif.). This area is reviewed in         Martin, Y. C., “3D Database Searching in Drug Design”, J. Med.         Chem., 35, pp. 2145-2154 (1992)).     -   3. HOOK (available from Molecular Simulations, Burlington,         Mass.).

Instead of proceeding to build a MurG inhibitor in a step-wise fashion one fragment or chemical entity at a time as described above, inhibitory or other MurG binding compounds may be designed as a whole or “de novo” using either an empty active site or optionally including some portion(s) of a known inhibitor(s). These methods include, but are not limited to:

-   -   1. LUDI (Bohm, H.-J., “The Computer Program LUDI: A New Method         for the De Novo Design of Enzyme Inhibitors”, J. ComR. Aid.         Molec. Design, 6, pp. 61-78 (1992)). LUDI is available from         Biosym Technologies, San Diego, Calif.     -   2. LEGEND (Nishibata, Y. and A. Itai, Tetrahedron, 47, p. 8985         (1991)). LEGEND is available from Molecular Simulations,         Burlington, Mass.     -   3. LeapFrog (available from Tripos Associates, St. Louis, Mo.).

Other molecular modeling techniques may also be employed in accordance with this invention. See, e.g., Cohen, N. C. et al., “Molecular Modeling Software and Methods for Medicinal Chemistry”, J. Med. Chem., 33, pp. 883-894 (1990). See also, Navia, M. A. and M. A. Mureko, “The Use of Structural Information in Drug Design”, Current Opinions in Structural Biology, 2, pp. 202-210 (1992).

Once a compound has been designed or selected by the above methods, the efficiency with which that compound may bind to MurG may be tested and optimized by computational evaluation. For example, a compound that has been designed or selected to function as a MurG-inhibitor must also preferably traverse a volume not overlapping that occupied by the active site when it is bound to the native substrate. An effective MurG inhibitor must preferably demonstrate a relatively small difference in energy between its bound and free states (i.e., a small deformation energy of binding). Thus, the most efficient MurG inhibitors should preferably be designed with a deformation energy of binding of not greater than about 10 kcal/mole, preferably, not greater than 7 kcal/mole. MurG inhibitors may interact with the enzyme in more than one conformation that is similar in overall binding energy. In those cases, thc deformation energy of binding is taken to be the difference between the energy of the free compound and the average energy of the conformations observed when the inhibitor binds to the enzyme.

A compound designed or selected as binding to MurG may be further computationally optimized so that in its bound state it would preferably lack repulsive electrostatic interaction with the target enzyme. Such non-complementary (e.g., electrostatic) interactions include repulsive charge-charge, dipole-dipole and charge-dipole interactions. Specifically, the sum of all electrostatic interactions between the inhibitor and the enzyme when the inhibitor is bound to MurG, preferably make a neutral or favorable contribution to the enthalpy of binding.

Specific computer software is available in the art to evaluate compound deformation energy and electrostatic interaction. Examples of programs designed for such uses include, but are not limited to: Gaussian 92, revision C [M. J. Frisch, Gaussian, Inc., Pittsburgh, Pa. COPYRIGHT. 1992]; AMBER, version 4.0 [P. A. Kollman, University of California at San Francisco, COPYRIGHT. 1994]; QUANTA/CHARMM [Molecular Simulations, Inc., Burlington, Mass. COPYRIGHT. 1994]; and Insight II/Discover (Biosysm Technologies Inc., San Diego, Calif. COPYRIGHT. 1994). These programs may be implemented, for instance, using a Silicon Graphics workstation, IRIS Octane or IBM RISC/6000 workstation. Other hardware systems and software packages will be known to those skilled in the art.

Once a MurG-binding compound has been optimally selected or designed, as described above, substitutions may then be made in some of its atoms or side groups in order to improve or modify its binding properties. Generally, initial substitutions are conservative, i.e., the replacement group will have approximately the same size, shape, hydrophobicity and charge as the original group. It should, of course, be understood that components known in the art to alter conformation should be avoided. Such substituted chemical compounds may then be analyzed for efficiency of fit to MurG by the same computer methods described in detail, above.

Compounds and Compositions Comprising Compounds Derived from Structure Based Drug Design

One embodiment of the present invention is a compound that is capable of binding to a MurG protein, inhibiting the activity of a MurG protein, or stimulating the activity of a MurG protein. Suitable inhibitory compounds of the present invention can: (1) inhibit (i.e., prevent or block) the activity of MurG enzyme by binding to a MurG donor nucleotide binding site and interfering with the binding of the donor nucleotide molecule; (2) inhibit the activity of MurG enzyme by binding to the MurG acceptor binding site and interfering with the binding of the acceptor molecule; (3) inhibit the activity of a MurG enzyme by binding to the membrane association site and interfering with the association of the protein with the bacterial membrane and/or acceptor molecule.

Another embodiment of the present invention is a compound that is capable of stimulating MurG activity. Suitable stimulatory compounds of the present invention can stimulate the activity of a MurG enzyme by binding to the protein at a binding site and causing an increase in enzymatic activity, for example, by increasing the enzymes affinity to bind a donor nucleotide, an acceptor molecule or improve the enzymes stability or increasing the binding affinity of a molecule to MurG.

Such compounds that bind to, inhibit or stimulate activity of a MurG protein include, for example, compounds that mimic donor nucleotide molecules. In preferred embodiments, the compound includes, for example, pyrimidine nucleoside analogues. In yet another preferred embodiment, the compounds include compounds comprising a pyrimidine nucleoside with a substituent containing at least one heteroatom attached to the C5 hydroxyl. In more particular embodiments, pyrimidine derivatives make complementary hydrogen bonding contacts to the amide backbone segment containing Ile 245 and also contact glutamate 269.

Another embodiment of the present invention is a compound that binds to the acceptor binding site of the MurG protein, hereinafter referred to a acceptor analogs. An acceptor analog refers to a compound that interacts with (e.g., binds to, associates with, modifies) the acceptor binding site of a MurG protein. An acceptor analog, for example, is a compound that mimics the natural acceptor molecule, Lipid I. Examples of such acceptor analogs are set forth in Ha et al., J. Amer. Chem. Soc. 1999, and PCT/US99/02187, U.S. Provisional Application No. 60/073,376 filed Feb. 2, 1998, incorporated herein by reference.

Another embodiment of the present invention is a compound that binds to the MurG protein, that are enzyme product analogs, hereinafter referred to as Lipid I analogs. A Lipid II analog refers to a compound that interacts with (i.e., binds to, associates with, modifies) the acceptor binding site of a Mur G protein which mimics the product of the transglycosylase reaction.

Inhibitory and stimulatory compounds of the present invention can be identified by various means known to those of skill in the art. For example, binding of an inhibitory compound to, or otherwise interaction with, a MurG protein, can be determined with MurG in solution, for example, using assays described in PCT/US99/02187, U.S. Provisional Application No. 60/073,376 filed Feb. 2, 1998, and PCT/US00/05554, U.S. Provisional Application Nos. 60/122,966 and 60/137,696, incorporated herein by reference.

According to the present invention, suitable compounds of the present invention include peptides or other organic molecules, and inorganic molecules. Suitable organic molecules include small organic molecules. Preferably, a compound of the present invention is not harmful (i.e., toxic) to an animal when administered to an animal.

Compounds of the present invention also can be identified using structure based drug design techniques known to those skilled in the art and described herein above.

Also according to the present invention, compounds are suitable for use in the inhibition of bacterial or microbial growth in an animal, and for example, function as an antibiotic for treatment of bacterial infections in animals.

The present invention also includes compositions comprising compounds of the present invention that inhibit or stimulate MurG activity which function as antibiotics or antimicrobial agents in animals. Compositions of the present invention can be used therapeutically or diagnostically in an animal. Compositions of the present invention comprises at least one compound of the present invention. In a preferred embodiment, compositions of the present invention further comprise a carrier. More particularly, a suitable carrier is a pharmaceutically acceptable carrier known to those skilled in the art.

TABLE 1 ATOMIC COORDINATES OF E. COLI MURG PROTEIN REMARK coordinates from minimization refinementREMARK refinement resolution: 40.0-1.9 AREMARK starting r = 0.2200 free_r = 0.2466REMARK final r = 0.2200 free_r = 0.2466REMARK rmsd bonds = 0.005558 rmsd angles = 1.29505REMARK wa = 1.08391REMARK target = mlf cycles = 1 steps = 30REMARK sg = P1 a = 60.613 b = 66.356 c = 67.902 alpha = 64.294 beta = 83.520 gamma = 65.448REMARK parameter file 1: CNS_TOPPAR: protein_rep.paramREMARK parameter file 2: CNS_TOPPAR: water_rep.paramREMARK parameter file 3: CNS_TOPPAR: ion_paramREMARK molecular structure file: gen.mtfREMARK input coordinates: gen.pdbREMARK reflection file = native.cvREMARK ncs = noneREMARK B-correction resolution: 6.0-1.9REMARK initial B-factor correction applied to fobs: REMARK B11 = 0.747 B22 = 2.098 B33 = 2.845REMARK B12 = −1.847 B13 = −3.752 B23 = 6.401REMARK B-factor correction applied to coordinate array B: 0.038REMARK bulk solvent: density level = 0.351665 e/A{circumflex over ( )}3, B-factor = 43.8282 A{circumflex over ( )}2REMARK reflections with |Fobs|/sigma_F < 2.0 rejectedREMARK reflections with |Fobs| > 10000 * rms(Fobs) rejectedREMARK theoretical total number of refl. in resol. range: 68102 (100.0%)REMARK number of unobserved reflections (no entry or |F| = 0): 2825 (4.1%) REMARK number of reflections rejected: 3288 (4.8%)REMARK total number of reflections used: 61989 91.0%)REMARK number of reflections in working set: 55765 (81.9%)REMARK number of reflections in test set: 6224 (9.1%)CRYST1 60.613 66.356 67.902 64.29 83.52 65.45 P 1 REMARK FILENAME = “minimize5.pdb” REMARK DATE: Jan. 14, 2000 15:25:36 created by user: shaREMARK VERSION: 0.5 ATOM 1 CB LYS A 7 0.142 3.434 35.023 1.00 43.02 AAAA ATOM 2 CG LYS A 7 1.076 4.457 35.641 1.00 46.34 AAAA ATOM 3 CD LYS A 7 0.452 5.841 35.634 1.00 47.39 AAAA ATOM 4 CE LYS A 7 1.345 6.846 36.332 1.00 48.65 AAAA ATOM 5 NZ LYS A 7 0.780 8.221 36.276 1.00 51.04 AAAA ATOM 6 C LYS A 7 − 2.239 2.733 34.833 1.00 39.64 AAAA ATOM 7 O LYS A 7 − 2.050 1.717 34.160 1.00 39.64 AAAA ATOM 8 N LYS A 7 − 0.974 2.320 36.947 1.00 42.05 AAAA ATOM 9 CA LYS A 7 − 1.170 3.245 35.788 1.00 41.31 AAAA ATOM 10 N ARG A 8 − 3.357 3.451 34.773 1.00 37.24 AAAA ATOM 11 CA ARG A 8 − 4.469 3.076 33.906 1.00 34.91 AAAA ATOM 12 CB ARG A 8 − 5.782 3.109 34.686 1.00 36.65 AAAA ATOM 13 CG ARG A 8 − 5.950 2.017 35.721 1.00 39.89 AAAA ATOM 14 CD ARG A 8 − 7.323 2.124 36.356 1.00 42.12 AAAA ATOM 15 NE ARG A 8 − 7.663 0.960 37.163 1.00 45.03 AAAA ATOM 16 CZ ARG A 8 − 7.031 0.610 38.279 1.00 46.29 AAAA ATOM 17 NH1 ARG A 8 − 6.015 1.337 38.725 1.00 46.88 AAAA ATOM 18 NH2 ARG A 8 − 7.420 −0.466 38.952 1.00 47.41 AAAA ATOM 19 C ARG A 8 − 4.584 3.999 32.696 1.00 32.27 AAAA ATOM 20 O ARG A 8 − 4.602 5.224 32.832 1.00 31.60 AAAA ATOM 21 N LEU A 9 − 4.663 3.403 31.512 1.00 29.57 AAAA ATOM 22 CA LEU A 9 − 4.792 4.171 30.283 1.00 27.45 AAAA ATOM 23 CB LEU A 9 − 3.581 3.954 29.362 1.00 26.31 AAAA ATOM 24 CG LEU A 9 − 3.752 4.466 27.916 1.00 25.77 AAAA ATOM 25 CD1 LEU A 9 − 3.670 5.985 27.895 1.00 24.31 AAAA ATOM 26 CD2 LEU A 9 −2.679 3.870 26.993 1.00 26.22 AAAA ATOM 27 C LEU A 9 −6.038 3.762 29.523 1.00 25.97 AAAA ATOM 28 O LEU A 9 −6.397 2.587 29.485 1.00 25.57 AAAA ATOM 29 N MET A 10 −6.713 4.738 28.928 1.00 25.37 AAAA ATOM 30 CA MET A 10 −7.866 4.429 28.101 1.00 24.70 AAAA ATOM 31 CB MET A 10 −9.142 5.101 28.612 1.00 25.60 AAAA ATOM 32 CG MET A 10 −10.323 4.873 27.675 1.00 25.77 AAAA ATOM 33 SD MET A 10 −11.916 4.958 28.492 1.00 26.63 AAAA ATOM 34 CE MET A 10 −12.197 3.222 28.862 1.00 25.72 AAAA ATOM 35 C MET A 10 −7.528 4.943 26.715 1.00 23.31 AAAA ATOM 36 O MET A 10 −7.198 6.116 26.544 1.00 24.02 AAAA ATOM 37 N VAL A 11 −7.574 4.059 25.727 1.00 22.25 AAAA ATOM 38 CA VAL A 11 −7.278 4.461 24.359 1.00 22.34 AAAA ATOM 39 CB VAL A 11 −6.444 3.386 23.624 1.00 22.75 AAAA ATOM 40 CG1 VAL A 11 −6.256 3.768 22.158 1.00 20.51 AAAA ATOM 41 CG2 VAL A 11 −5.082 3.239 24.310 1.00 21.75 AAAA ATOM 42 C VAL A 11 −8.612 4.654 23.646 1.00 22.94 AAAA ATOM 43 O VAL A 11 −9.525 3.843 23.804 1.00 23.37 AAAA ATOM 44 N MET A 12 −8.722 5.734 22.878 1.00 22.18 AAAA ATOM 45 CA MET A 12 −9.949 6.034 22.146 1.00 23.10 AAAA ATOM 46 CB MET A 12 −10.496 7.399 22.589 1.00 22.78 AAAA ATOM 47 CG MET A 12 −10.359 7.655 24.096 1.00 23.92 AAAA ATOM 48 SD MET A 12 −10.955 9.279 24.657 1.00 25.51 AAAA ATOM 49 CE MET A 12 −9.641 10.349 24.162 1.00 22.79 AAAA ATOM 50 C MET A 12 −9.582 6.072 20.673 1.00 22.97 AAAA ATOM 51 O MET A 12 −8.917 6.997 20.226 1.00 21.16 AAAA ATOM 52 N ALA A 13 −9.992 5.057 19.921 1.00 26.97 AAAA ATOM 53 CA ALA A 13 −9.665 5.008 18.498 1.00 30.88 AAAA ATOM 54 CB ALA A 13 −8.381 4.212 18.288 1.00 31.18 AAAA ATOM 55 C ALA A 13 −10.813 4.412 17.685 1.00 34.35 AAAA ATOM 56 O ALA A 13 −11.328 3.335 18.006 1.00 35.86 AAAA ATOM 57 N GLY A 14 −11.176 5.127 16.622 1.00 37.37 AAAA ATOM 58 CA GLY A 14 −12.287 4.762 15.757 1.00 40.54 AAAA ATOM 59 C GLY A 14 −12.239 3.583 14.808 1.00 41.52 AAAA ATOM 60 O GLY A 14 −11.267 2.831 14.755 1.00 43.26 AAAA ATOM 61 N GLY A 15 −13.322 3.451 14.042 1.00 42.70 AAAA ATOM 62 CA GLY A 15 −13.491 2.363 13.094 1.00 43.13 AAAA ATOM 63 C GLY A 15 −12.660 2.286 11.825 1.00 43.41 AAAA ATOM 64 O GLY A 15 −13.212 2.187 10.730 1.00 44.39 AAAA ATOM 65 N THR A 16 −11.340 2.333 11.966 1.00 43.38 AAAA ATOM 66 CA THR A 16 −10.426 2.204 10.833 1.00 43.22 AAAA ATOM 67 CB THR A 16 −10.120 3.551 10.110 1.00 44.23 AAAA ATOM 68 OG1 THR A 16 −9.302 4.375 10.949 1.00 44.41 AAAA ATOM 69 CG2 THR A 16 −11.404 4.286 9.754 1.00 43.74 AAAA ATOM 70 C THR A 16 −9.118 1.679 11.402 1.00 43.06 AAAA ATOM 71 O THR A 16 −8.728 2.042 12.517 1.00 42.99 AAAA ATOM 72 N GLY A 17 −8.453 0.810 10.649 1.00 41.81 AAAA ATOM 73 CA GLY A 17 −7.190 0.268 11.109 1.00 40.71 AAAA ATOM 74 C GLY A 17 −6.202 1.401 11.275 1.00 39.54 AAAA ATOM 75 O GLY A 17 −5.275 1.330 12.085 1.00 39.73 AAAA ATOM 76 N GLY A 18 −6.413 2.460 10.500 1.00 37.79 AAAA ATOM 77 CA GLY A 18 −5.539 3.611 10.572 1.00 35.68 AAAA ATOM 78 C GLY A 18 −5.394 4.116 11.994 1.00 34.88 AAAA ATOM 79 O GLY A 18 −4.285 4.441 12.427 1.00 35.21 AAAA ATOM 80 N HIS A 19 −6.503 4.186 12.728 1.00 32.89 AAAA ATOM 81 CA HIS A 19 −6.454 4.664 14.110 1.00 32.14 AAAA ATOM 82 CB HIS A 19 −7.759 5.371 14.504 1.00 30.28 AAAA ATOM 83 CG HIS A 19 −8.150 6.504 13.605 1.00 28.85 AAAA ATOM 84 CD2 HIS A 19 −9.336 6.808 13.027 1.00 27.83 AAAA ATOM 85 ND1 HIS A 19 −7.288 7.524 13.265 1.00 28.68 AAAA ATOM 86 CE1 HIS A 19 −7.926 8.407 12.517 1.00 28.09 AAAA ATOM 87 NE2 HIS A 19 −9.170 7.996 12.358 1.00 27.45 AAAA ATOM 88 C HIS A 19 −6.229 3.533 15.108 1.00 31.91 AAAA ATOM 89 O HIS A 19 −5.480 3.684 16.072 1.00 31.76 AAAA ATOM 90 N VAL A 20 −6.895 2.407 14.881 1.00 31.82 AAAA ATOM 91 CA VAL A 20 −6.813 1.271 15.788 1.00 33.08 AAAA ATOM 92 CB VAL A 20 −7.875 0.215 15.430 1.00 33.31 AAAA ATOM 93 CG1 VAL A 20 −7.766 −0.982 16.361 1.00 33.91 AAAA ATOM 94 CG2 VAL A 20 −9.260 0.830 15.540 1.00 34.25 AAAA ATOM 95 C VAL A 20 −5.452 0.587 15.898 1.00 33.31 AAAA ATOM 96 O VAL A 20 −4.977 0.337 17.008 1.00 32.99 AAAA ATOM 97 N PHE A 21 −4.823 0.288 14.765 1.00 33.64 AAAA ATOM 98 CA PHE A 21 −3.526 −0.385 14.794 1.00 33.68 AAAA ATOM 99 CB PHE A 21 −3.020 −0.648 13.368 1.00 35.58 AAAA ATOM 100 CG PHE A 21 −3.900 −1.578 12.577 1.00 39.10 AAAA ATOM 101 CD1 PHE A 21 −4.463 −2.701 13.174 1.00 40.50 AAAA ATOM 102 CD2 PHE A 21 −4.157 −1.338 11.232 1.00 41.05 AAAA ATOM 103 CE1 PHE A 21 −5.271 −3.572 12.446 1.00 41.55 AAAA ATOM 104 CE2 PHE A 21 −4.964 −2.205 10.492 1.00 41.86 AAAA ATOM 105 CZ PHE A 21 −5.521 −3.323 11.103 1.00 42.12 AAAA ATOM 106 C PHE A 21 −2.456 0.350 15.605 1.00 32.04 AAAA ATOM 107 O PHE A 21 −1.789 −0.257 16.443 1.00 31.30 AAAA ATOM 108 N PRO A 22 −2.277 1.662 15.375 1.00 31.37 AAAA ATOM 109 CD PRO A 22 −2.939 2.544 14.400 1.00 31.41 AAAA ATOM 110 CA PRO A 22 −1.259 2.396 16.139 1.00 30.01 AAAA ATOM 111 CB PRO A 22 −1.301 3.799 15.536 1.00 30.97 AAAA ATOM 112 CG PRO A 22 −1.892 3.592 14.175 1.00 31.19 AAAA ATOM 113 C PRO A 22 −1.620 2.411 17.624 1.00 29.31 AAAA ATOM 114 O PRO A 22 −0.749 2.366 18.489 1.00 27.42 AAAA ATOM 115 N GLY A 23 −2.918 2.483 17.903 1.00 28.99 AAAA ATOM 116 CA GLY A 23 −3.380 2.492 19.277 1.00 28.59 AAAA ATOM 117 C GLY A 23 −3.035 1.196 19.990 1.00 29.00 AAAA ATOM 118 O GLY A 23 −2.649 1.205 21.160 1.00 28.48 AAAA ATOM 119 N LEU A 24 −3.168 0.078 19.282 1.00 28.08 AAAA ATOM 120 CA LEU A 24 −2.863 −1.227 19.859 1.00 28.39 AAAA ATOM 121 CB LEU A 24 −3.306 −2.347 18.913 1.00 28.16 AAAA ATOM 122 CG LEU A 24 −4.811 −2.605 18.843 1.00 28.45 AAAA ATOM 123 CD1 LEU A 24 −5.117 −3.583 17.714 1.00 29.25 AAAA ATOM 124 CD2 LEU A 24 −5.291 −3.158 20.181 1.00 29.35 AAAA ATOM 125 C LEU A 24 −1.373 −1.350 20.147 1.00 28.37 AAAA ATOM 126 O LEU A 24 −0.966 −1.986 21.126 1.00 28.60 AAAA ATOM 127 N ALA A 25 −0.555 −0.743 19.296 1.00 27.77 AAAA ATOM 128 CA ALA A 25 0.887 −0.795 19.497 1.00 28.98 AAAA ATOM 129 CB ALA A 25 1.616 −0.142 18.321 1.00 27.53 AAAA ATOM 130 C ALA A 25 1.256 −0.093 20.800 1.00 29.10 AAAA ATOM 131 O ALA A 25 2.035 −0.618 21.595 1.00 29.49 AAAA ATOM 132 N VAL A 26 0.694 1.094 21.020 1.00 28.82 AAAA ATOM 133 CA VAL A 26 0.982 1.853 22.233 1.00 28.94 AAAA ATOM 134 CB VAL A 26 0.400 3.290 22.157 1.00 29.74 AAAA ATOM 135 CG1 VAL A 26 0.691 4.049 23.454 1.00 29.76 AAAA ATOM 136 CG2 VAL A 26 1.009 4.026 20.981 1.00 29.14 AAAA ATOM 137 C VAL A 26 0.409 1.131 23.450 1.00 29.18 AAAA ATOM 138 O VAL A 26 1.020 1.118 24.518 1.00 29.62 AAAA ATOM 139 N ALA A 27 −0.757 0.518 23.286 1.00 27.98 AAAA ATOM 140 CA ALA A 27 −1.371 −0.215 24.382 1.00 29.32 AAAA ATOM 141 CB ALA A 27 −2.719 −0.755 23.950 1.00 28.32 AAAA ATOM 142 C ALA A 27 −0.462 −1.372 24.840 1.00 30.04 AAAA ATOM 143 O ALA A 27 −0.084 −1.454 26.015 1.00 29.89 AAAA ATOM 144 N HIS A 28 −0.120 −2.259 23.907 1.00 30.92 AAAA ATOM 145 CA HIS A 28 0.734 −3.413 24.201 1.00 30.62 AAAA ATOM 146 CB HIS A 28 1.024 −4.214 22.924 1.00 30.20 AAAA ATOM 147 CG HIS A 28 −0.112 −5.080 22.483 1.00 31.65 AAAA ATOM 148 CD2 HIS A 28 −0.764 −5.162 21.299 1.00 31.33 AAAA ATOM 149 ND1 HIS A 28 −0.717 −5.996 23.319 1.00 31.81 AAAA ATOM 150 CE1 HIS A 28 −1.696 −6.600 22.670 1.00 32.38 AAAA ATOM 151 NE2 HIS A 28 −1.747 −6.112 21.443 1.00 32.85 AAAA ATOM 152 C HIS A 28 2.054 −2.989 24.823 1.00 30.90 AAAA ATOM 153 O HIS A 28 2.537 −3.601 25.779 1.00 30.92 AAAA ATOM 154 N HIS A 29 2.636 −1.939 24.263 1.00 30.28 AAAA ATOM 155 CA HIS A 29 3.899 −1.415 24.742 1.00 30.76 AAAA ATOM 156 CB HIS A 29 4.276 −0.195 23.911 1.00 31.40 AAAA ATOM 157 CG HIS A 29 5.679 0.274 24.122 1.00 33.14 AAAA ATOM 158 CD2 HIS A 29 6.188 1.226 24.939 1.00 33.77 AAAA ATOM 159 ND1 HIS A 29 6.748 −0.240 23.420 1.00 34.47 AAAA ATOM 160 CE1 HIS A 29 7.855 0.381 23.791 1.00 34.76 AAAA ATOM 161 NE2 HIS A 29 7.542 1.275 24.711 1.00 34.09 AAAA ATOM 162 C HIS A 29 3.835 −1.032 26.227 1.00 31.63 AAAA ATOM 163 O HIS A 29 4.763 −1.315 26.990 1.00 30.76 AAAA ATOM 164 N LEU A 30 2.744 −0.388 26.638 1.00 29.72 AAAA ATOM 165 CA LEU A 30 2.603 0.035 28.028 1.00 30.08 AAAA ATOM 166 CB LEU A 30 1.631 1.225 28.126 1.00 29.45 AAAA ATOM 167 CG LEU A 30 2.107 2.503 27.420 1.00 28.69 AAAA ATOM 168 CD1 LEU A 30 1.026 3.587 27.477 1.00 27.76 AAAA ATOM 169 CD2 LEU A 30 3.383 2.998 28.075 1.00 28.99 AAAA ATOM 170 C LEU A 30 2.153 −1.096 28.950 1.00 30.55 AAAA ATOM 171 O LEU A 30 2.538 −1.136 30.120 1.00 31.28 AAAA ATOM 172 N MET A 31 1.340 −2.012 28.438 1.00 31.26 AAAA ATOM 173 CA MET A 31 0.884 −3.130 29.256 1.00 33.71 AAAA ATOM 174 CB MET A 31 −0.118 −3.999 28.494 1.00 34.12 AAAA ATOM 175 CG MET A 31 −1.452 −3.341 28.249 1.00 34.98 AAAA ATOM 176 SD MET A 31 −2.618 −4.475 27.485 1.00 38.51 AAAA ATOM 177 CE MET A 31 −2.086 −4.401 25.803 1.00 37.49 AAAA ATOM 178 C MET A 31 2.078 −3.987 29.664 1.00 35.03 AAAA ATOM 179 O MET A 31 2.101 −4.548 30.758 1.00 36.09 AAAA ATOM 180 N ALA A 32 3.062 −4.085 28.776 1.00 35.62 AAAA ATOM 181 CA ALA A 32 4.262 −4.871 29.044 1.00 37.61 AAAA ATOM 182 CB ALA A 32 5.049 −5.087 27.755 1.00 37.79 AAAA ATOM 183 C ALA A 32 5.133 −4.158 30.070 1.00 38.72 AAAA ATOM 184 O ALA A 32 6.223 −4.621 30.409 1.00 39.48 AAAA ATOM 185 N GLN A 33 4.654 −3.022 30.560 1.00 38.28 AAAA ATOM 186 CA GLN A 33 5.408 −2.275 31.548 1.00 38.14 AAAA ATOM 187 CB GLN A 33 5.903 −0.969 30.941 1.00 39.68 AAAA ATOM 188 CG GLN A 33 6.856 −1.210 29.791 1.00 42.76 AAAA ATOM 189 CD GLN A 33 7.262 0.061 29.096 1.00 44.20 AAAA ATOM 190 OE1 GLN A 33 7.803 0.975 29.717 1.00 46.28 AAAA ATOM 191 NE2 GLN A 33 7.002 0.131 27.795 1.00 44.60 AAAA ATOM 192 C GLN A 33 4.576 −2.020 32.787 1.00 36.68 AAAA ATOM 193 O GLN A 33 4.822 −1.075 33.532 1.00 37.34 AAAA ATOM 194 N GLY A 34 3.585 −2.877 33.000 1.00 35.86 AAAA ATOM 195 CA GLY A 34 2.738 −2.755 34.170 1.00 35.52 AAAA ATOM 196 C GLY A 34 1.461 −1.951 34.008 1.00 34.34 AAAA ATOM 197 O GLY A 34 0.611 −1.974 34.897 1.00 33.67 AAAA ATOM 198 N TRP A 35 1.314 −1.248 32.890 1.00 34.23 AAAA ATOM 199 CA TRP A 35 0.121 −0.435 32.661 1.00 33.63 AAAA ATOM 200 CB TRP A 35 0.324 0.509 31.474 1.00 34.84 AAAA ATOM 201 CG TRP A 35 1.150 1.722 31.753 1.00 35.09 AAAA ATOM 202 CD2 TRP A 35 0.722 3.087 31.659 1.00 36.11 AAAA ATOM 203 CE2 TRP A 35 1.840 3.897 31.957 1.00 36.13 AAAA ATOM 204 CE3 TRP A 35 −0.499 3.705 31.350 1.00 37.33 AAAA ATOM 205 CD1 TRP A 35 2.469 1.759 32.099 1.00 35.78 AAAA ATOM 206 NE1 TRP A 35 2.893 3.062 32.221 1.00 34.49 AAAA ATOM 207 CZ2 TRP A 35 1.776 5.293 31.955 1.00 37.71 AAAA ATOM 208 CZ3 TRP A 35 −0.563 5.095 31.348 1.00 37.99 AAAA ATOM 209 CH2 TRP A 35 0.570 5.874 31.650 1.00 38.17 AAAA ATOM 210 C TRP A 35 −1.153 −1.228 32.402 1.00 33.77 AAAA ATOM 211 O TRP A 35 −1.136 −2.282 31.763 1.00 32.95 AAAA ATOM 212 N GLN A 36 −2.261 −0.704 32.912 1.00 32.90 AAAA ATOM 213 CA GLN A 36 −3.567 −1.301 32.696 1.00 33.08 AAAA ATOM 214 CB GLN A 36 −4.448 −1.160 33.937 1.00 34.93 AAAA ATOM 215 CG GLN A 36 −4.240 −2.228 34.992 1.00 38.58 AAAA ATOM 216 CD GLN A 36 −5.272 −2.143 36.103 1.00 40.36 AAAA ATOM 217 OE1 GLN A 36 −5.295 −1.186 36.874 1.00 42.12 AAAA ATOM 218 NE2 GLN A 36 −6.140 −3.146 36.181 1.00 42.80 AAAA ATOM 219 C GLN A 36 −4.160 −0.482 31.552 1.00 32.42 AAAA ATOM 220 O GLN A 36 −4.114 0.748 31.583 1.00 31.42 AAAA ATOM 221 N VAL A 37 −4.697 −1.157 30.541 1.00 32.07 AAAA ATOM 222 CA VAL A 37 −5.276 −0.456 29.403 1.00 31.91 AAAA ATOM 223 CB VAL A 37 −4.436 −0.656 28.123 1.00 32.46 AAAA ATOM 224 CG1 VAL A 37 −5.010 0.179 26.983 1.00 32.66 AAAA ATOM 225 CG2 VAL A 37 −2.994 −0.269 28.379 1.00 31.40 AAAA ATOM 226 C VAL A 37 −6.693 −0.917 29.118 1.00 32.15 AAAA ATOM 227 O VAL A 37 −7.017 −2.104 29.225 1.00 31.04 AAAA ATOM 228 N ARG A 38 −7.532 0.046 28.752 1.00 30.74 AAAA ATOM 229 CA ARG A 38 −8.925 −0.202 28.433 1.00 31.08 AAAA ATOM 230 CB ARG A 38 −9.807 0.325 29.562 1.00 33.01 AAAA ATOM 231 CG ARG A 38 −11.251 −0.116 29.499 1.00 37.13 AAAA ATOM 232 CD ARG A 38 −11.532 −1.185 30.529 1.00 39.30 AAAA ATOM 233 NE ARG A 38 −12.937 −1.567 30.519 1.00 41.65 AAAA ATOM 234 CZ ARG A 38 −13.464 −2.495 31.308 1.00 43.12 AAAA ATOM 235 NH1 ARG A 38 −12.697 −3.142 32.176 1.00 43.84 AAAA ATOM 236 NH2 ARG A 38 −14.758 −2.773 31.227 1.00 43.90 AAAA ATOM 237 C ARG A 38 −9.196 0.568 27.143 1.00 29.87 AAAA ATOM 238 O ARG A 38 −8.574 1.601 26.883 1.00 28.94 AAAA ATOM 239 N TRP A 39 −10.119 0.072 26.332 1.00 28.69 AAAA ATOM 240 CA TRP A 39 −10.414 0.729 25.071 1.00 28.19 AAAA ATOM 241 CB TRP A 39 −10.321 −0.305 23.939 1.00 29.84 AAAA ATOM 242 CG TRP A 39 −10.046 0.269 22.583 1.00 33.23 AAAA ATOM 243 CD2 TRP A 39 −8.774 0.339 21.919 1.00 33.62 AAAA ATOM 244 CE2 TRP A 39 −8.995 0.945 20.661 1.00 34.00 AAAA ATOM 245 CE3 TRP A 39 −7.470 −0.052 22.261 1.00 33.80 AAAA ATOM 246 CD1 TRP A 39 −10.955 0.823 21.729 1.00 34.36 AAAA ATOM 247 NE1 TRP A 39 −10.332 1.230 20.573 1.00 33.43 AAAA ATOM 248 CZ2 TRP A 39 −7.960 1.171 19.743 1.00 34.56 AAAA ATOM 249 CZ3 TRP A 39 −6.442 0.171 21.350 1.00 35.28 AAAA ATOM 250 CH2 TRP A 39 −6.695 0.779 20.102 1.00 34.47 AAAA ATOM 251 C TRP A 39 −11.790 1.395 25.081 1.00 26.35 AAAA ATOM 252 O TRP A 39 −12.683 0.994 25.826 1.00 26.68 AAAA ATOM 253 N LEU A 40 −11.935 2.438 24.269 1.00 25.04 AAAA ATOM 254 CA LEU A 40 −13.197 3.159 24.130 1.00 23.18 AAAA ATOM 255 CB LEU A 40 −13.074 4.602 24.637 1.00 22.55 AAAA ATOM 256 CG LEU A 40 −14.395 5.381 24.623 1.00 20.79 AAAA ATOM 257 CD1 LEU A 40 −15.314 4.801 25.675 1.00 21.21 AAAA ATOM 258 CD2 LEU A 40 −14.149 6.868 24.905 1.00 21.72 AAAA ATOM 259 C LEU A 40 −13.495 3.179 22.634 1.00 22.87 AAAA ATOM 260 O LEU A 40 −12.718 3.721 21.854 1.00 22.99 AAAA ATOM 261 N GLY A 41 −14.608 2.580 22.232 1.00 25.02 AAAA ATOM 262 CA GLY A 41 −14.946 2.553 20.821 1.00 25.95 AAAA ATOM 263 C GLY A 41 −16.426 2.332 20.594 1.00 28.01 AAAA ATOM 264 O GLY A 41 −17.234 2.555 21.494 1.00 28.82 AAAA ATOM 265 N THR A 42 −16.783 1.884 19.395 1.00 29.77 AAAA ATOM 266 CA THR A 42 −18.185 1.641 19.059 1.00 31.41 AAAA ATOM 267 CB THR A 42 −18.603 2.497 17.855 1.00 32.12 AAAA ATOM 268 OG1 THR A 42 −18.293 3.871 18.119 1.00 34.95 AAAA ATOM 269 CG2 THR A 42 −20.098 2.367 17.611 1.00 34.55 AAAA ATOM 270 C THR A 42 −18.458 0.168 18.741 1.00 32.23 AAAA ATOM 271 O THR A 42 −17.721 −0.463 17.986 1.00 29.57 AAAA ATOM 272 N ALA A 43 −19.541 −0.360 19.306 1.00 34.77 AAAA ATOM 273 CA ALA A 43 −19.920 −1.760 19.127 1.00 37.23 AAAA ATOM 274 CB ALA A 43 −21.173 −2.060 19.948 1.00 37.66 AAAA ATOM 275 C ALA A 43 −20.126 −2.232 17.686 1.00 39.10 AAAA ATOM 276 O ALA A 43 −20.088 −3.434 17.422 1.00 39.09 AAAA ATOM 277 N ASP A 44 −20.333 −1.304 16.757 1.00 40.78 AAAA ATOM 278 CA ASP A 44 −20.557 −1.671 15.361 1.00 42.78 AAAA ATOM 279 CB ASP A 44 −21.678 −0.812 14.774 1.00 44.80 AAAA ATOM 280 CG ASP A 44 −21.438 0.670 14.973 1.00 46.37 AAAA ATOM 281 OD1 ASP A 44 −20.464 1.206 14.400 1.00 48.22 AAAA ATOM 282 OD2 ASP A 44 −22.220 1.302 15.712 1.00 49.14 AAAA ATOM 283 C ASP A 44 −19.324 −1.559 14.472 1.00 43.14 AAAA ATOM 284 O ASP A 44 −19.320 −2.061 13.349 1.00 44.14 AAAA ATOM 285 N ARG A 45 −18.281 −0.904 14.970 1.00 42.77 AAAA ATOM 286 CA ARG A 45 −17.056 −0.730 14.199 1.00 42.34 AAAA ATOM 287 CB ARG A 45 −16.415 0.614 14.550 1.00 44.43 AAAA ATOM 288 CG ARG A 45 −17.206 1.822 14.056 1.00 48.23 AAAA ATOM 289 CD ARG A 45 −17.272 1.845 12.533 1.00 51.20 AAAA ATOM 290 NE ARG A 45 −17.950 3.029 12.014 1.00 54.35 AAAA ATOM 291 CZ ARG A 45 −17.526 4.279 12.191 1.00 56.26 AAAA ATOM 292 NH1 ARG A 45 −16.417 4.522 12.881 1.00 56.45 AAAA ATOM 293 NH2 ARG A 45 −18.212 5.290 11.670 1.00 57.50 AAAA ATOM 294 C ARG A 45 −16.054 −1.872 14.401 1.00 41.11 AAAA ATOM 295 O ARG A 45 −16.194 −2.679 15.320 1.00 40.45 AAAA ATOM 296 N MET A 46 −15.041 −1.928 13.543 1.00 39.55 AAAA ATOM 297 CA MET A 46 −14.038 −2.990 13.604 1.00 39.67 AAAA ATOM 298 CB MET A 46 −13.041 −2.839 12.444 1.00 39.68 AAAA ATOM 299 CG MET A 46 −12.239 −1.544 12.423 1.00 42.15 AAAA ATOM 300 SD MET A 46 −10.690 −1.620 13.352 1.00 44.74 AAAA ATOM 301 CE MET A 46 −9.559 −2.332 12.128 1.00 41.92 AAAA ATOM 302 C MET A 46 −13.279 −3.148 14.926 1.00 38.68 AAAA ATOM 303 O MET A 46 −12.772 −4.232 15.219 1.00 38.02 AAAA ATOM 304 N GLU A 47 −13.198 −2.092 15.730 1.00 37.48 AAAA ATOM 305 CA GLU A 47 −12.486 −2.198 17.002 1.00 36.91 AAAA ATOM 306 CB GLU A 47 −12.309 −0.820 17.650 1.00 35.19 AAAA ATOM 307 CG GLU A 47 −13.615 −0.150 18.058 1.00 34.12 AAAA ATOM 308 CD GLU A 47 −14.142 0.807 17.003 1.00 34.06 AAAA ATOM 309 OE1 GLU A 47 −13.712 0.707 15.832 1.00 33.13 AAAA ATOM 310 OE2 GLU A 47 −14.995 1.652 17.350 1.00 32.08 AAAA ATOM 311 C GLU A 47 −13.225 −3.123 17.972 1.00 36.96 AAAA ATOM 312 O GLU A 47 −12.612 −3.744 18.842 1.00 37.00 AAAA ATOM 313 N ALA A 48 −14.541 −3.222 17.818 1.00 36.76 AAAA ATOM 314 CA ALA A 48 −15.342 −4.066 18.700 1.00 36.98 AAAA ATOM 315 CB ALA A 48 −16.823 −3.917 18.365 1.00 37.33 AAAA ATOM 316 C ALA A 48 −14.943 −5.533 18.623 1.00 38.23 AAAA ATOM 317 O ALA A 48 −15.100 −6.281 19.590 1.00 37.91 AAAA ATOM 318 N ASP A 49 −14.430 −5.947 17.470 1.00 39.31 AAAA ATOM 319 CA ASP A 49 −14.027 −7.332 17.286 1.00 40.97 AAAA ATOM 320 CB ASP A 49 −14.477 −7.832 15.909 1.00 42.68 AAAA ATOM 321 CG ASP A 49 −15.988 −7.912 15.783 1.00 44.91 AAAA ATOM 322 OD1 ASP A 49 −16.612 −8.681 16.549 1.00 45.64 AAAA ATOM 323 OD2 ASP A 49 −16.552 −7.205 14.918 1.00 46.44 AAAA ATOM 324 C ASP A 49 −12.524 −7.519 17.426 1.00 40.10 AAAA ATOM 325 O ASP A 49 −12.069 −8.518 17.974 1.00 40.92 AAAA ATOM 326 N LEU A 50 −11.761 −6.549 16.940 1.00 39.40 AAAA ATOM 327 CA LEU A 50 −10.306 −6.623 16.982 1.00 39.05 AAAA ATOM 328 CB LEU A 50 −9.710 −5.578 16.036 1.00 38.17 AAAA ATOM 329 CG LEU A 50 −8.183 −5.562 15.942 1.00 38.18 AAAA ATOM 330 CD1 LEU A 50 −7.685 −6.916 15.462 1.00 37.91 AAAA ATOM 331 CD2 LEU A 50 −7.740 −4.460 14.999 1.00 37.50 AAAA ATOM 332 C LEU A 50 −9.666 −6.486 18.365 1.00 39.12 AAAA ATOM 333 O LEU A 50 −8.805 −7.286 18.732 1.00 38.56 AAAA ATOM 334 N VAL A 51 −10.084 −5.483 19.132 1.00 38.79 AAAA ATOM 335 CA VAL A 51 −9.516 −5.257 20.459 1.00 37.64 AAAA ATOM 336 CB VAL A 51 −10.127 −3.989 21.111 1.00 36.87 AAAA ATOM 337 CG1 VAL A 51 −9.571 −3.795 22.523 1.00 35.15 AAAA ATOM 338 CG2 VAL A 51 −9.810 −2.777 20.256 1.00 34.42 AAAA ATOM 339 C VAL A 51 −9.647 −6.449 21.415 1.00 37.87 AAAA ATOM 340 O VAL A 51 −8.695 −6.790 22.115 1.00 37.54 AAAA ATOM 341 N PRO A 52 −10.825 −7.093 21.465 1.00 38.44 AAAA ATOM 342 CD PRO A 52 −12.141 −6.700 20.932 1.00 38.92 AAAA ATOM 343 CA PRO A 52 −10.959 −8.237 22.373 1.00 39.32 AAAA ATOM 344 CB PRO A 52 −12.436 −8.602 22.253 1.00 39.97 AAAA ATOM 345 CG PRO A 52 −13.080 −7.277 21.962 1.00 38.98 AAAA ATOM 346 C PRO A 52 −10.035 −9.392 21.974 1.00 40.07 AAAA ATOM 347 O PRO A 52 −9.685 −10.232 22.805 1.00 40.30 AAAA ATOM 348 N LYS A 53 −9.649 −9.427 20.699 1.00 40.35 AAAA ATOM 349 CA LYS A 53 −8.752 −10.463 20.193 1.00 40.58 AAAA ATOM 350 CB LYS A 53 −8.812 −10.541 18.661 1.00 41.25 AAAA ATOM 351 CG LYS A 53 −10.093 −11.169 18.129 1.00 43.24 AAAA ATOM 352 CD LYS A 53 −10.033 −11.383 16.627 1.00 44.40 AAAA ATOM 353 CE LYS A 53 −11.280 −12.102 16.133 1.00 45.87 AAAA ATOM 354 NZ LYS A 53 −11.250 −12.342 14.659 1.00 47.88 AAAA ATOM 355 C LYS A 53 −7.323 −10.184 20.636 1.00 39.99 AAAA ATOM 356 O LYS A 53 −6.426 −11.006 20.432 1.00 39.70 AAAA ATOM 357 N HIS A 54 −7.112 −9.014 21.231 1.00 38.65 AAAA ATOM 358 CA HIS A 54 −5.790 −8.642 21.727 1.00 37.71 AAAA ATOM 359 CB HIS A 54 −5.408 −7.233 21.272 1.00 37.50 AAAA ATOM 360 CG HIS A 54 −4.903 −7.164 19.864 1.00 37.59 AAAA ATOM 361 CD2 HIS A 54 −5.483 −7.502 18.687 1.00 37.67 AAAA ATOM 362 ND1 HIS A 54 −3.658 −6.666 19.546 1.00 37.90 AAAA ATOM 363 CE1 HIS A 54 −3.492 −6.698 18.235 1.00 37.11 AAAA ATOM 364 NE2 HIS A 54 −4.586 −7.202 17.691 1.00 36.75 AAAA ATOM 365 C HIS A 54 −5.788 −8.711 23.248 1.00 37.10 AAAA ATOM 366 O HIS A 54 −4.871 −8.214 23.899 1.00 37.35 AAAA ATOM 367 N GLY A 55 −6.828 −9.331 23.800 1.00 36.15 AAAA ATOM 368 CA GLY A 55 −6.948 −9.477 25.240 1.00 36.70 AAAA ATOM 369 C GLY A 55 −7.266 −8.200 25.997 1.00 36.66 AAAA ATOM 370 O GLY A 55 −7.145 −8.157 27.222 1.00 36.89 AAAA ATOM 371 N ILE A 56 −7.686 −7.163 25.277 1.00 35.61 AAAA ATOM 372 CA ILE A 56 −8.009 −5.885 25.900 1.00 34.03 AAAA ATOM 373 CB ILE A 56 −7.389 −4.723 25.100 1.00 32.39 AAAA ATOM 374 CG2 ILE A 56 −7.748 −3.386 25.750 1.00 31.80 AAAA ATOM 375 CG1 ILE A 56 −5.869 −4.904 25.031 1.00 31.50 AAAA ATOM 376 CD1 ILE A 56 −5.149 −3.900 24.144 1.00 30.46 AAAA ATOM 377 C ILE A 56 −9.516 −5.668 26.017 1.00 34.37 AAAA ATOM 378 O ILE A 56 −10.263 −5.908 25.067 1.00 34.29 AAAA ATOM 379 N GLU A 57 −9.955 −5.224 27.193 1.00 34.18 AAAA ATOM 380 CA GLU A 57 −11.370 −4.969 27.432 1.00 34.19 AAAA ATOM 381 CB GLU A 57 −11.638 −4.733 28.922 1.00 37.08 AAAA ATOM 382 CG GLU A 57 −11.301 −5.913 29.837 1.00 41.06 AAAA ATOM 383 CD GLU A 57 −12.180 −7.127 29.591 1.00 44.07 AAAA ATOM 384 OE1 GLU A 57 −12.011 −8.135 30.313 1.00 45.83 AAAA ATOM 385 OE2 GLU A 57 −13.040 −7.078 28.682 1.00 46.00 AAAA ATOM 386 C GLU A 57 −11.751 −3.723 26.645 1.00 32.88 AAAA ATOM 387 O GLU A 57 −10.905 −2.870 26.368 1.00 31.69 AAAA ATOM 388 N ILE A 58 −13.022 −3.611 26.285 1.00 31.36 AAAA ATOM 389 CA ILE A 58 −13.454 −2.454 25.529 1.00 29.92 AAAA ATOM 390 CB ILE A 58 −13.390 −2.749 24.009 1.00 29.51 AAAA ATOM 391 CG2 ILE A 58 −14.175 −4.015 23.689 1.00 28.67 AAAA ATOM 392 CG1 ILE A 58 −13.895 −1.543 23.216 1.00 29.61 AAAA ATOM 393 CD1 ILE A 58 −13.578 −1.623 21.734 1.00 29.09 AAAA ATOM 394 C ILE A 58 −14.843 −1.984 25.927 1.00 29.49 AAAA ATOM 395 O ILE A 58 −15.791 −2.764 25.968 1.00 27.83 AAAA ATOM 396 N ASP A 59 −14.939 −0.700 26.252 1.00 29.28 AAAA ATOM 397 CA ASP A 59 −16.202 −0.091 26.626 1.00 29.70 AAAA ATOM 398 CB ASP A 59 −15.999 0.916 27.759 1.00 30.90 AAAA ATOM 399 CG ASP A 59 −15.676 0.245 29.083 1.00 32.17 AAAA ATOM 400 OD1 ASP A 59 −16.485 −0.591 29.540 1.00 33.00 AAAA ATOM 401 OD2 ASP A 59 −14.615 0.554 29.664 1.00 33.03 AAAA ATOM 402 C ASP A 59 −16.723 0.608 25.378 1.00 30.39 AAAA ATOM 403 O ASP A 59 −15.947 1.165 24.600 1.00 30.45 AAAA ATOM 404 N PHE A 60 −18.033 0.570 25.180 1.00 31.29 AAAA ATOM 405 CA PHE A 60 −18.612 1.183 24.000 1.00 32.36 AAAA ATOM 406 CB PHE A 60 −19.469 0.166 23.239 1.00 33.01 AAAA ATOM 407 CG PHE A 60 −18.720 −1.056 22.793 1.00 33.55 AAAA ATOM 408 CD1 PHE A 60 −19.033 −2.307 23.318 1.00 34.07 AAAA ATOM 409 CD2 PHE A 60 −17.720 −0.964 21.832 1.00 34.02 AAAA ATOM 410 CE1 PHE A 60 −18.362 −3.451 22.890 1.00 33.73 AAAA ATOM 411 CE2 PHE A 60 −17.042 −2.104 21.397 1.00 34.93 AAAA ATOM 412 CZ PHE A 60 −17.366 −3.348 21.928 1.00 34.12 AAAA ATOM 413 C PHE A 60 −19.469 2.395 24.300 1.00 32.89 AAAA ATOM 414 O PHE A 60 −20.062 2.508 25.372 1.00 33.13 AAAA ATOM 415 N ILE A 61 −19.502 3.309 23.338 1.00 34.43 AAAA ATOM 416 CA ILE A 61 −20.326 4.500 23.421 1.00 36.08 AAAA ATOM 417 CB ILE A 61 −19.545 5.785 23.056 1.00 36.15 AAAA ATOM 418 CG2 ILE A 61 −20.511 6.957 22.913 1.00 36.47 AAAA ATOM 419 CG1 ILE A 61 −18.504 6.092 24.136 1.00 37.27 AAAA ATOM 420 CD1 ILE A 61 −17.711 7.360 23.875 1.00 38.32 AAAA ATOM 421 C ILE A 61 −21.380 4.230 22.353 1.00 37.27 AAAA ATOM 422 O ILE A 61 −21.050 3.901 21.215 1.00 36.29 AAAA ATOM 423 N ARG A 62 −22.644 4.337 22.728 1.00 39.91 AAAA ATOM 424 CA ARG A 62 −23.732 4.087 21.797 1.00 43.16 AAAA ATOM 425 CB ARG A 62 −24.818 3.268 22.494 1.00 44.19 AAAA ATOM 426 CG ARG A 62 −26.183 3.312 21.825 1.00 48.33 AAAA ATOM 427 CD ARG A 62 −27.207 2.581 22.680 1.00 50.28 AAAA ATOM 428 NE ARG A 62 −28.584 2.906 22.319 1.00 52.71 AAAA ATOM 429 CZ ARG A 62 −29.646 2.419 22.951 1.00 53.14 AAAA ATOM 430 NH1 ARG A 62 −29.482 1.586 23.968 1.00 54.03 AAAA ATOM 431 NH2 ARG A 62 −30.870 2.767 22.573 1.00 53.49 AAAA ATOM 432 C ARG A 62 −24.302 5.400 21.280 1.00 44.33 AAAA ATOM 433 O ARG A 62 −24.942 6.140 22.021 1.00 43.98 AAAA ATOM 434 N ILE A 63 −24.053 5.686 20.005 1.00 46.60 AAAA ATOM 435 CA ILE A 63 −24.537 6.912 19.378 1.00 49.26 AAAA ATOM 436 CB ILE A 63 −23.369 7.834 18.965 1.00 49.17 AAAA ATOM 437 CG2 ILE A 63 −23.903 9.208 18.593 1.00 50.31 AAAA ATOM 438 CG1 ILE A 63 −22.368 7.967 20.113 1.00 49.48 AAAA ATOM 439 CD1 ILE A 63 −21.158 8.822 19.775 1.00 49.03 AAAA ATOM 440 C ILE A 63 −25.316 6.540 18.123 1.00 50.72 AAAA ATOM 441 O ILE A 63 −24.724 6.219 17.093 1.00 50.90 AAAA ATOM 442 N SER A 64 −26.639 6.591 18.209 1.00 52.58 AAAA ATOM 443 CA SER A 64 −27.488 6.235 17.078 1.00 54.45 AAAA ATOM 444 CB SER A 64 −28.731 5.491 17.574 1.00 54.65 AAAA ATOM 445 OG SER A 64 −29.528 6.329 18.391 1.00 55.29 AAAA ATOM 446 C SER A 64 −27.927 7.433 16.242 1.00 55.33 AAAA ATOM 447 O SER A 64 −27.919 8.571 16.713 1.00 55.34 AAAA ATOM 448 N GLY A 65 −28.301 7.158 14.993 1.00 56.31 AAAA ATOM 449 CA GLY A 65 −28.774 8.196 14.090 1.00 57.42 AAAA ATOM 450 C GLY A 65 −27.751 9.156 13.508 1.00 58.34 AAAA ATOM 451 O GLY A 65 −28.052 10.333 13.315 1.00 58.53 AAAA ATOM 452 N LEU A 66 −26.552 8.668 13.207 1.00 59.08 AAAA ATOM 453 CA LEU A 66 −25.514 9.530 12.648 1.00 59.80 AAAA ATOM 454 CB LEU A 66 −24.147 9.153 13.229 1.00 59.99 AAAA ATOM 455 CG LEU A 66 −23.927 9.513 14.704 1.00 60.38 AAAA ATOM 456 CD1 LEU A 66 −23.983 11.026 14.877 1.00 60.37 AAAA ATOM 457 CD2 LEU A 66 −24.983 8.840 15.565 1.00 60.47 AAAA ATOM 458 C LEU A 66 −25.467 9.497 11.121 1.00 60.04 AAAA ATOM 459 O LEU A 66 −25.049 10.466 10.484 1.00 59.29 AAAA ATOM 460 N ARG A 67 −25.892 8.378 10.541 1.00 60.97 AAAA ATOM 461 CA ARG A 67 −25.923 8.224 9.089 1.00 61.57 AAAA ATOM 462 CB ARG A 67 −26.860 9.273 8.484 1.00 62.96 AAAA ATOM 463 CG ARG A 67 −28.340 8.984 8.698 1.00 65.29 AAAA ATOM 464 CD ARG A 67 −29.138 10.270 8.842 1.00 66.93 AAAA ATOM 465 NE ARG A 67 −30.566 10.067 8.611 1.00 68.58 AAAA ATOM 466 CZ ARG A 67 −31.514 10.924 8.980 1.00 69.56 AAAA ATOM 467 NH1 ARG A 67 −31.192 12.048 9.607 1.00 69.39 AAAA ATOM 468 NH2 ARG A 67 −32.788 10.665 8.709 1.00 69.97 AAAA ATOM 469 C ARG A 67 −24.558 8.301 8.409 1.00 61.08 AAAA ATOM 470 O ARG A 67 −24.474 8.448 7.191 1.00 61.57 AAAA ATOM 471 N GLY A 68 −23.489 8.204 9.189 1.00 60.22 AAAA ATOM 472 CA GLY A 68 −22.161 8.249 8.605 1.00 58.95 AAAA ATOM 473 C GLY A 68 −21.531 9.627 8.541 1.00 58.19 AAAA ATOM 474 O GLY A 68 −20.373 9.763 8.140 1.00 58.31 AAAA ATOM 475 N LYS A 69 −22.282 10.655 8.921 1.00 57.03 AAAA ATOM 476 CA LYS A 69 −21.746 12.009 8.904 1.00 55.91 AAAA ATOM 477 CB LYS A 69 −22.812 13.015 9.349 1.00 56.90 AAAA ATOM 478 CG LYS A 69 −23.827 13.368 8.264 1.00 57.91 AAAA ATOM 479 CD LYS A 69 −23.167 14.147 7.133 1.00 58.56 AAAA ATOM 480 CE LYS A 69 −24.163 14.517 6.044 1.00 59.37 AAAA ATOM 481 NZ LYS A 69 −23.522 15.327 4.965 1.00 59.41 AAAA ATOM 482 C LYS A 69 −20.527 12.078 9.818 1.00 54.19 AAAA ATOM 483 O LYS A 69 −19.447 12.480 9.392 1.00 54.69 AAAA ATOM 484 N GLY A 70 −20.697 11.676 11.072 1.00 51.77 AAAA ATOM 485 CA GLY A 70 −19.575 11.692 11.991 1.00 48.95 AAAA ATOM 486 C GLY A 70 −19.668 12.687 13.129 1.00 46.84 AAAA ATOM 487 O GLY A 70 −20.754 12.975 13.629 1.00 46.29 AAAA ATOM 488 N ILE A 71 −18.515 13.221 13.523 1.00 45.26 AAAA ATOM 489 CA ILE A 71 −18.415 14.174 14.623 1.00 43.82 AAAA ATOM 490 CB ILE A 71 −16.936 14.463 14.959 1.00 42.91 AAAA ATOM 491 CG2 ILE A 71 −16.262 15.142 13.786 1.00 42.86 AAAA ATOM 492 CG1 ILE A 71 −16.839 15.325 16.217 1.00 41.89 AAAA ATOM 493 CD1 ILE A 71 −17.324 14.619 17.471 1.00 42.12 AAAA ATOM 494 C ILE A 71 −19.127 15.501 14.367 1.00 43.91 AAAA ATOM 495 O ILE A 71 −19.635 16.125 15.296 1.00 43.71 AAAA ATOM 496 N LYS A 72 −19.154 15.935 13.112 1.00 43.92 AAAA ATOM 497 CA LYS A 72 −19.815 17.188 12.757 1.00 43.85 AAAA ATOM 498 CB LYS A 72 −19.559 17.526 11.284 1.00 45.17 AAAA ATOM 499 CG LYS A 72 −20.140 16.517 10.297 1.00 46.64 AAAA ATOM 500 CD LYS A 72 −19.590 15.112 10.516 1.00 47.65 AAAA ATOM 501 CE LYS A 72 −18.070 15.074 10.388 1.00 47.12 AAAA ATOM 502 NZ LYS A 72 −17.533 13.692 10.506 1.00 46.69 AAAA ATOM 503 C LYS A 72 −21.318 17.073 13.003 1.00 42.82 AAAA ATOM 504 O LYS A 72 −21.969 18.035 13.414 1.00 43.31 AAAA ATOM 505 N ALA A 73 −21.862 15.889 12.752 1.00 41.38 AAAA ATOM 506 CA ALA A 73 −23.282 15.650 12.954 1.00 39.79 AAAA ATOM 507 CB ALA A 73 −23.700 14.379 12.238 1.00 39.55 AAAA ATOM 508 C ALA A 73 −23.575 15.524 14.438 1.00 39.28 AAAA ATOM 509 O ALA A 73 −24.509 16.132 14.959 1.00 37.60 AAAA ATOM 510 N LEU A 74 −22.760 14.725 15.116 1.00 38.96 AAAA ATOM 511 CA LEU A 74 −22.933 14.498 16.541 1.00 38.75 AAAA ATOM 512 CB LEU A 74 −21.817 13.575 17.055 1.00 39.47 AAAA ATOM 513 CG LEU A 74 −21.826 13.192 18.536 1.00 39.30 AAAA ATOM 514 CD1 LEU A 74 −21.439 14.383 19.366 1.00 40.12 AAAA ATOM 515 CD2 LEU A 74 −23.199 12.673 18.936 1.00 39.66 AAAA ATOM 516 C LEU A 74 −22.938 15.808 17.317 1.00 38.15 AAAA ATOM 517 O LEU A 74 −23.768 16.012 18.206 1.00 37.74 AAAA ATOM 518 N ILE A 75 −22.014 16.699 16.982 1.00 38.08 AAAA ATOM 519 CA ILE A 75 −21.923 17.975 17.678 1.00 39.02 AAAA ATOM 520 CB ILE A 75 −20.605 18.707 17.319 1.00 40.76 AAAA ATOM 521 CG2 ILE A 75 −20.616 19.109 15.856 1.00 41.16 AAAA ATOM 522 CD1 ILE A 75 −20.426 19.938 18.209 1.00 42.50 AAAA ATOM 523 CD1 ILE A 75 −20.302 19.616 19.690 1.00 44.15 AAAA ATOM 524 C ILE A 75 −23.114 18.886 17.377 1.00 38.41 AAAA ATOM 525 O ILE A 75 −23.396 19.818 18.130 1.00 38.12 AAAA ATOM 526 N ALA A 76 −23.816 18.602 16.283 1.00 38.04 AAAA ATOM 527 CA ALA A 76 −24.971 19.399 15.878 1.00 37.19 AAAA ATOM 528 CB ALA A 76 −25.060 19.454 14.350 1.00 37.36 AAAA ATOM 529 C ALA A 76 −26.268 18.847 16.455 1.00 36.15 AAAA ATOM 530 O ALA A 76 −27.352 19.323 16.124 1.00 35.97 AAAA ATOM 531 N ALA A 77 −26.156 17.834 17.309 1.00 34.42 AAAA ATOM 532 CA ALA A 77 −27.326 17.225 17.935 1.00 33.14 AAAA ATOM 533 CB ALA A 77 −27.460 15.780 17.499 1.00 33.13 AAAA ATOM 534 C ALA A 77 −27.125 17.311 19.443 1.00 32.59 AAAA ATOM 535 O ALA A 77 −26.502 16.436 20.042 1.00 31.09 AAAA ATOM 536 N PRO A 78 −27.664 18.372 20.073 1.00 32.06 AAAA ATOM 537 CD PRO A 78 −28.619 19.290 19.423 1.00 31.98 AAAA ATOM 538 CA PRO A 78 −27.577 18.653 21.514 1.00 31.07 AAAA ATOM 539 CB PRO A 78 −28.671 19.701 21.727 1.00 32.32 AAAA ATOM 540 CG PRO A 78 −28.703 20.427 20.414 1.00 32.04 AAAA ATOM 541 C PRO A 78 −27.748 17.450 22.443 1.00 30.50 AAAA ATOM 542 O PRO A 78 −26.874 17.155 23.257 1.00 29.52 AAAA ATOM 543 N LEU A 79 −28.878 16.766 22.334 1.00 28.95 AAAA ATOM 544 CA LEU A 79 −29.130 15.619 23.194 1.00 29.33 AAAA ATOM 545 CB LEU A 79 −30.573 15.137 23.023 1.00 29.48 AAAA ATOM 546 CG LEU A 79 −31.644 16.154 23.435 1.00 30.82 AAAA ATOM 547 CD1 LEU A 79 −33.025 15.542 23.234 1.00 31.23 AAAA ATOM 548 CD2 LEU A 79 −31.450 16.558 24.901 1.00 30.46 AAAA ATOM 549 C LEU A 79 −28.160 14.465 22.950 1.00 28.58 AAAA ATOM 550 O LEU A 79 −27.745 13.795 23.898 1.00 27.00 AAAA ATOM 551 N ARG A 80 −27.794 14.240 21.689 1.00 27.70 AAAA ATOM 552 CA ARG A 80 −26.877 13.156 21.348 1.00 28.33 AAAA ATOM 553 CB ARG A 80 −26.813 12.941 19.836 1.00 30.44 AAAA ATOM 554 CG ARG A 80 −28.037 12.294 19.222 1.00 36.59 AAAA ATOM 555 CD ARG A 80 −27.657 11.616 17.915 1.00 38.91 AAAA ATOM 556 NE ARG A 80 −28.821 11.189 17.151 1.00 43.51 AAAA ATOM 557 CZ ARG A 80 −29.537 11.991 16.370 1.00 44.36 AAAA ATOM 558 NH1 ARG A 80 −29.207 13.270 16.244 1.00 45.19 AAAA ATOM 559 NH2 ARG A 80 −30.589 11.513 15.721 1.00 45.91 AAAA ATOM 560 C ARG A 80 −25.464 13.384 21.871 1.00 27.39 AAAA ATOM 561 O ARG A 80 −24.835 12.455 22.392 1.00 26.07 AAAA ATOM 562 N ILE A 81 −24.950 14.603 21.719 1.00 26.19 AAAA ATOM 563 CA ILE A 81 −23.608 14.886 22.217 1.00 24.89 AAAA ATOM 564 CB ILE A 81 −23.081 16.269 21.702 1.00 25.72 AAAA ATOM 565 CG2 ILE A 81 −24.069 17.373 22.021 1.00 26.90 AAAA ATOM 566 CG1 ILE A 81 −21.722 16.584 22.332 1.00 25.98 AAAA ATOM 567 CD1 ILE A 81 −20.696 15.474 22.169 1.00 26.39 AAAA ATOM 568 C ILE A 81 −23.609 14.832 23.752 1.00 24.30 AAAA ATOM 569 O ILE A 81 −22.669 14.315 24.365 1.00 22.57 AAAA ATOM 570 N ILE A 82 −24.672 15.344 24.367 1.00 22.71 AAAA ATOM 571 CA PHE A 82 −24.800 15.333 25.827 1.00 22.28 AAAA ATOM 572 CB PHE A 82 −26.099 16.029 26.236 1.00 21.54 AAAA ATOM 573 CG PHE A 82 −26.281 16.184 27.730 1.00 20.67 AAAA ATOM 574 CD1 PHE A 82 −25.244 16.644 28.538 1.00 21.08 AAAA ATOM 575 CD2 PHE A 82 −27.512 15.907 28.318 1.00 21.44 AAAA ATOM 576 CE1 PHE A 82 −25.430 16.831 29.916 1.00 20.18 AAAA ATOM 577 CH2 PHE A 82 −27.719 16.093 29.700 1.00 19.77 AAAA ATOM 578 CZ PHE A 82 −26.678 16.555 30.497 1.00 20.80 AAAA ATOM 579 C PHE A 82 −24.797 13.887 26.330 1.00 21.61 AAAA ATOM 580 O PHE A 82 −24.091 13.536 27.285 1.00 21.05 AAAA ATOM 581 N ASN A 83 −25.577 13.042 25.669 1.00 21.80 AAAA ATOM 582 CA ASN A 83 −25.648 11.640 26.045 1.00 22.62 AAAA ATOM 583 CB ASN A 83 −26.806 10.969 25.296 1.00 22.62 AAAA ATOM 584 CG ASN A 83 −26.921 9.495 25.612 1.00 25.00 AAAA ATOM 585 OD1 ASN A 83 −26.227 8.677 25.031 1.00 26.80 AAAA ATOM 586 ND2 ASN A 83 −27.791 9.153 26.548 1.00 28.27 AAAA ATOM 587 C ASN A 83 −24.324 10.888 25.805 1.00 21.61 AAAA ATOM 588 O ASN A 83 −23.903 10.080 26.639 1.00 22.04 AAAA ATOM 589 N ALA A 84 −23.658 11.150 24.686 1.00 19.98 AAAA ATOM 590 CA ALA A 84 −22.383 10.480 24.401 1.00 19.25 AAAA ATOM 591 CB ALA A 84 −21.912 10.817 22.981 1.00 20.79 AAAA ATOM 592 C ALA A 84 −21.318 10.906 25.424 1.00 19.48 AAAA ATOM 593 O ALA A 84 −20.509 10.095 25.880 1.00 18.26 AAAA ATOM 594 N TRP A 85 −21.322 12.188 25.769 1.00 17.57 AAAA ATOM 595 CA TRP A 85 −20.390 12.736 26.749 1.00 18.15 AAAA ATOM 596 CB TRP A 85 −20.561 14.260 26.781 1.00 17.16 AAAA ATOM 597 CG TRP A 85 −19.863 15.007 27.892 1.00 16.32 AAAA ATOM 598 CD2 TRP A 85 −20.300 16.233 28.472 1.00 16.29 AAAA ATOM 599 CE2 TRP A 85 −19.340 16.605 29.445 1.00 15.39 AAAA ATOM 600 CE3 TRP A 85 −21.413 17.062 28.266 1.00 16.28 AAAA ATOM 601 CD1 TRP A 85 −18.677 14.682 28.519 1.00 15.58 AAAA ATOM 602 NE1 TRP A 85 −18.364 15.639 29.454 1.00 14.76 AAAA ATOM 603 CZ2 TRP A 85 −19.458 17.762 30.204 1.00 14.50 AAAA ATOM 604 CZ3 TRP A 85 −21.530 18.218 29.027 1.00 16.55 AAAA ATOM 605 CH2 TRP A 85 −20.553 18.558 29.988 1.00 15.65 AAAA ATOM 606 C TRP A 85 −20.639 12.099 28.125 1.00 19.04 AAAA ATOM 607 O TRP A 85 −19.696 11.691 28.820 1.00 17.64 AAAA ATOM 608 N ARG A 86 −21.903 11.986 28.516 1.00 18.52 AAAA ATOM 609 CA ARG A 86 −22.216 11.375 29.803 1.00 19.34 AAAA ATOM 610 CB ARG A 86 −23.675 11.654 30.181 1.00 19.24 AAAA ATOM 611 CG ARG A 86 −23.892 13.104 30.660 1.00 18.36 AAAA ATOM 612 CD ARG A 86 −25.318 13.357 31.154 1.00 19.61 AAAA ATOM 613 NE ARG A 86 −26.303 13.245 30.072 1.00 19.64 AAAA ATOM 614 CZ ARG A 86 −27.021 12.156 29.807 1.00 21.06 AAAA ATOM 615 NH1 ARG A 86 −26.880 11.063 30.548 1.00 19.09 AAAA ATOM 616 NH2 ARG A 86 −27.879 12.156 28.787 1.00 18.59 AAAA ATOM 627 O GLN A 87 −19.846 6.687 29.576 1.00 18.93 AAAA ATOM 628 N ALA A 88 −19.471 8.479 28.255 1.00 20.24 AAAA ATOM 629 CA ALA A 88 −18.023 8.436 28.412 1.00 20.23 AAAA ATOM 630 CB ALA A 88 −17.355 9.386 27.419 1.00 18.84 AAAA ATOM 631 C ALA A 88 −17.622 8.787 29.841 1.00 20.11 AAAA ATOM 632 O ALA A 88 −16.687 8.202 30.388 1.00 20.39 AAAA ATOM 633 N ARG A 89 −18.309 9.745 30.454 1.00 18.15 AAAA ATOM 634 CA ARG A 89 −17.985 10.091 31.836 1.00 19.16 AAAA ATOM 635 CB ARG A 89 −18.797 11.302 32.313 1.00 16.58 AAAA ATOM 636 CG ARG A 89 −18.225 12.657 31.896 1.00 17.41 AAAA ATOM 637 CD ARG A 89 −19.196 13.769 32.284 1.00 15.10 AAAA ATOM 638 NE ARG A 89 −19.437 13.835 33.729 1.00 16.60 AAAA ATOM 639 CZ ARG A 89 −18.675 14.506 34.587 1.00 16.76 AAAA ATOM 640 NH1 ARG A 89 −17.609 15.173 34.157 1.00 16.02 AAAA ATOM 641 NH2 ARG A 89 −18.990 14.531 35.877 1.00 15.64 AAAA ATOM 642 C ARG A 89 −18.258 8.902 32.764 1.00 19.91 AAAA ATOM 643 O ARG A 89 −17.469 8.618 33.674 1.00 18.92 AAAA ATOM 644 N ALA A 90 −19.371 8.213 32.544 1.00 21.12 AAAA ATOM 645 CA ALA A 90 −19.719 7.063 33.386 1.00 23.31 AAAA ATOM 646 CB ALA A 90 −21.080 6.502 32.976 1.00 24.02 AAAA ATOM 647 C ALA A 90 −18.640 5.990 33.257 1.00 24.57 AAAA ATOM 648 O ALA A 90 −18.236 5.367 34.243 1.00 24.35 AAAA ATOM 649 N ILE A 91 −18.173 5.790 32.031 1.00 24.03 AAAA ATOM 650 CA ILE A 91 −17.135 4.816 31.746 1.00 24.73 AAAA ATOM 651 CB ILE A 91 −16.922 4.699 30.209 1.00 25.99 AAAA ATOM 652 CG2 ILE A 91 −15.547 4.086 29.890 1.00 25.27 AAAA ATOM 653 CG1 ILE A 91 −18.061 3.875 29.601 1.00 25.74 AAAA ATOM 654 CD1 ILE A 91 −18.123 3.931 28.085 1.00 25.37 AAAA ATOM 655 C ILE A 91 −15.823 5.196 32.436 1.00 25.69 AAAA ATOM 656 O ILE A 91 −15.133 4.339 32.991 1.00 25.17 AAAA ATOM 657 N MET A 92 −15.482 6.481 32.410 1.00 24.39 AAAA ATOM 658 CA MET A 92 −14.243 6.933 33.024 1.00 24.61 AAAA ATOM 659 CB MET A 92 −13.798 8.258 32.391 1.00 23.19 AAAA ATOM 660 CG MET A 92 −13.480 8.088 30.908 1.00 21.54 AAAA ATOM 661 SD MET A 92 −12.816 9.554 30.108 1.00 21.51 AAAA ATOM 662 CE MET A 92 −12.756 9.008 28.463 1.00 17.14 AAAA ATOM 663 C MET A 92 −14.325 7.041 34.545 1.00 24.72 AAAA ATOM 664 O MET A 92 −13.311 6.918 35.236 1.00 24.71 AAAA ATOM 665 N LYS A 93 −15.524 7.262 35.070 1.00 24.64 AAAA ATOM 666 CA LYS A 93 −15.700 7.337 36.517 1.00 26.89 AAAA ATOM 667 CB LYS A 93 −17.102 7.840 36.864 1.00 27.06 AAAA ATOM 668 CG LYS A 93 −17.269 9.345 36.831 1.00 26.10 AAAA ATOM 669 CD LYS A 93 −18.641 9.742 37.366 1.00 28.56 AAAA ATOM 670 CE LYS A 93 −18.762 11.251 37.483 1.00 28.03 AAAA ATOM 671 NZ LYS A 93 −20.068 11.663 38.060 1.00 29.77 AAAA ATOM 672 C LYS A 93 −15.495 5.938 37.119 1.00 28.19 AAAA ATOM 673 O LYS A 93 −14.994 5.792 38.238 1.00 28.43 AAAA ATOM 674 N ALA A 94 −15.880 4.912 36.367 1.00 29.30 AAAA ATOM 675 CA ALA A 94 −15.736 3.532 36.831 1.00 30.63 AAAA ATOM 676 CB ALA A 94 −16.750 2.635 36.131 1.00 30.03 AAAA ATOM 677 C ALA A 94 −14.325 2.981 36.622 1.00 30.40 AAAA ATOM 678 O ALA A 94 −13.778 2.322 37.507 1.00 30.67 AAAA ATOM 679 N TYR A 95 −13.735 3.255 35.462 1.00 29.39 AAAA ATOM 680 CA TYR A 95 −12.394 2.764 35.163 1.00 29.94 AAAA ATOM 681 CB TYR A 95 −12.189 2.685 33.648 1.00 29.85 AAAA ATOM 682 CG TYR A 95 −10.838 2.151 33.224 1.00 31.64 AAAA ATOM 683 CD1 TYR A 95 −10.382 0.907 33.669 1.00 31.90 AAAA ATOM 684 CE1 TYR A 95 −9.139 0.414 33.270 1.00 32.14 AAAA ATOM 685 CD2 TYR A 95 −10.015 2.886 32.370 1.00 30.90 AAAA ATOM 686 CE2 TYR A 95 −8.779 2.405 31.969 1.00 31.95 AAAA ATOM 687 CZ TYR A 95 −8.345 1.167 32.423 1.00 32.95 AAAA ATOM 688 OH TYR A 95 −7.120 0.687 32.019 1.00 33.09 AAAA ATOM 689 C TYR A 95 −11.312 3.633 35.791 1.00 29.90 AAAA ATOM 690 O TYR A 95 −10.253 3.137 36.190 1.00 28.99 AAAA ATOM 691 N LYS A 96 −11.584 4.930 35.871 1.00 28.94 AAAA ATOM 692 CA LYS A 96 −10.658 5.893 36.452 1.00 29.17 AAAA ATOM 693 CB LYS A 96 −10.543 5.658 37.966 1.00 32.14 AAAA ATOM 694 CG LYS A 96 −11.871 5.829 38.690 1.00 35.57 AAAA ATOM 695 CD LYS A 96 −11.784 5.541 40.183 1.00 38.37 AAAA ATOM 696 CE LYS A 96 −13.158 5.718 40.828 1.00 39.96 AAAA ATOM 697 NZ LYS A 96 −13.170 5.428 42.295 1.00 42.96 AAAA ATOM 698 C LYS A 96 −9.274 5.884 35.817 1.00 27.78 AAAA ATOM 699 O LYS A 96 −8.281 5.608 36.482 1.00 28.12 AAAA ATOM 700 N PRO A 97 −9.187 6.185 34.509 1.00 26.15 AAAA ATOM 701 CD PRO A 97 −10.258 6.519 33.547 1.00 24.76 AAAA ATOM 702 CA PRO A 97 −7.867 6.191 33.868 1.00 24.70 AAAA ATOM 703 CB PRO A 97 −8.202 6.241 32.381 1.00 23.96 AAAA ATOM 704 CG PRO A 97 −9.477 7.078 32.362 1.00 24.55 AAAA ATOM 705 C PRO A 97 −7.060 7.408 34.320 1.00 24.77 AAAA ATOM 706 O PRO A 97 −7.628 8.438 34.684 1.00 23.93 AAAA ATOM 707 N ASP A 98 −5.737 7.288 34.314 1.00 24.94 AAAA ATOM 708 CA ASP A 98 −4.890 8.404 34.717 1.00 24.75 AAAA ATOM 709 CB ASP A 98 −3.554 7.891 35.261 1.00 26.69 AAAA ATOM 710 CG ASP A 98 −3.725 7.040 36.509 1.00 28.25 AAAA ATOM 711 OD1 ASP A 98 −3.546 5.808 36.426 1.00 28.34 AAAA ATOM 712 OD2 ASP A 98 −4.053 7.603 37.569 1.00 29.50 AAAA ATOM 713 C ASP A 98 −4.654 9.328 33.529 1.00 23.89 AAAA ATOM 714 O ASP A 98 −4.267 10.486 33.681 1.00 22.57 AAAA ATOM 715 N VAL A 99 −4.918 8.807 32.339 1.00 24.10 AAAA ATOM 716 CA VAL A 99 −4.740 9.569 31.111 1.00 23.85 AAAA ATOM 717 CB VAL A 99 −3.237 9.633 30.730 1.00 25.11 AAAA ATOM 718 CG1 VAL A 99 −2.684 8.220 30.614 1.00 25.72 AAAA ATOM 719 CG2 VAL A 99 −3.044 10.372 29.420 1.00 24.76 AAAA ATOM 720 C VAL A 99 −5.498 8.865 29.989 1.00 22.90 AAAA ATOM 721 O VAL A 99 −5.767 7.667 30.073 1.00 22.05 AAAA ATOM 722 N VAL A 100 −5.869 9.613 28.951 1.00 22.07 AAAA ATOM 723 CA VAL A 100 −6.544 9.008 27.808 1.00 21.38 AAAA ATOM 724 CB VAL A 100 −8.038 9.451 27.663 1.00 21.17 AAAA ATOM 725 CG1 VAL A 100 −8.804 9.095 28.914 1.00 21.06 AAAA ATOM 726 CG2 VAL A 100 −8.139 10.942 27.354 1.00 22.14 AAAA ATOM 727 C VAL A 100 −5.777 9.398 26.559 1.00 21.31 AAAA ATOM 728 O VAL A 100 −5.244 10.505 26.464 1.00 21.01 AAAA ATOM 729 N LEU A 101 −5.701 8.468 25.612 1.00 21.54 AAAA ATOM 730 CA LEU A 101 −4.994 8.697 24.362 1.00 22.01 AAAA ATOM 731 CB LEU A 101 −3.944 7.599 24.139 1.00 23.42 AAAA ATOM 732 CG LEU A 101 −2.691 7.856 23.288 1.00 25.21 AAAA ATOM 733 CD1 LEU A 101 −2.230 6.515 22.696 1.00 25.87 AAAA ATOM 734 CD2 LEU A 101 −2.930 8.854 22.187 1.00 26.43 AAAA ATOM 735 C LEU A 101 −6.006 8.644 23.222 1.00 21.51 AAAA ATOM 736 O LEU A 101 −6.667 7.625 23.029 1.00 21.94 AAAA ATOM 737 N GLY A 102 −6.127 9.742 22.484 1.00 21.18 AAAA ATOM 738 CA GLY A 102 −7.043 9.780 21.358 1.00 21.84 AAAA ATOM 739 C GLY A 102 −6.246 9.586 20.079 1.00 21.20 AAAA ATOM 740 O GLY A 102 −5.294 10.324 19.837 1.00 22.62 AAAA ATOM 741 N MET A 103 −6.627 8.599 19.270 1.00 21.18 AAAA ATOM 742 CA MET A 103 −5.933 8.312 18.015 1.00 22.83 AAAA ATOM 743 CB MET A 103 −5.715 6.805 17.865 1.00 23.16 AAAA ATOM 744 CG MET A 103 −4.978 6.140 19.030 1.00 24.31 AAAA ATOM 745 SD MET A 103 −3.333 6.804 19.308 1.00 27.62 AAAA ATOM 746 CE MET A 103 −2.455 6.156 17.873 1.00 26.43 AAAA ATOM 747 C MET A 103 −6.709 8.823 16.795 1.00 23.47 AAAA ATOM 748 O MET A 103 −6.351 8.532 15.653 1.00 23.75 AAAA ATOM 749 N GLY A 104 −7.767 9.590 17.043 1.00 25.38 AAAA ATOM 750 CA GLY A 104 −8.585 10.114 15.959 1.00 25.56 AAAA ATOM 751 C GLY A 104 −9.878 9.326 15.833 1.00 25.55 AAAA ATOM 752 O GLY A 104 −10.004 8.241 16.404 1.00 26.58 AAAA ATOM 753 N GLY A 105 −10.840 9.854 15.082 1.00 26.06 AAAA ATOM 754 CA GLY A 105 −12.107 9.159 14.930 1.00 26.21 AAAA ATOM 755 C GLY A 105 −13.140 9.819 15.823 1.00 26.96 AAAA ATOM 756 O GLY A 105 −12.810 10.258 16.926 1.00 25.49 AAAA ATOM 757 N TYR A 106 −14.393 9.863 15.376 1.00 27.65 AAAA ATOM 758 CA TYR A 106 −15.434 10.534 16.145 1.00 28.10 AAAA ATOM 759 CB TYR A 106 −16.759 10.556 15.362 1.00 31.05 AAAA ATOM 760 CG TYR A 106 −17.536 9.257 15.303 1.00 33.49 AAAA ATOM 761 CD1 TYR A 106 −18.269 8.802 16.400 1.00 34.81 AAAA ATOM 762 CE1 TYR A 106 −19.038 7.634 16.323 1.00 36.18 AAAA ATOM 763 CD2 TYR A 106 −17.581 8.509 14.123 1.00 35.64 AAAA ATOM 764 CE2 TYR A 106 −18.343 7.344 14.032 1.00 36.47 AAAA ATOM 765 CZ TYR A 106 −19.069 6.912 15.133 1.00 37.27 AAAA ATOM 766 OH TYR A 106 −19.829 5.766 15.027 1.00 38.99 AAAA ATOM 767 C TYR A 106 −15.678 10.072 17.576 1.00 26.46 AAAA ATOM 768 O TYR A 106 −15.976 10.897 18.430 1.00 26.55 AAAA ATOM 769 N VAL A 107 −15.549 8.780 17.858 1.00 25.31 AAAA ATOM 770 CA VAL A 107 −15.783 8.318 19.223 1.00 23.91 AAAA ATOM 771 CB VAL A 107 −15.659 6.772 19.335 1.00 25.47 AAAA ATOM 772 CG1 VAL A 107 −14.224 6.327 19.076 1.00 26.57 AAAA ATOM 773 CG2 VAL A 107 −16.126 6.315 20.711 1.00 24.96 AAAA ATOM 774 C VAL A 107 −14.836 8.993 20.223 1.00 23.22 AAAA ATOM 775 O VAL A 107 −15.190 9.190 21.389 1.00 23.17 AAAA ATOM 776 N SER A 108 −13.650 9.381 19.765 1.00 23.13 AAAA ATOM 777 CA SER A 108 −12.676 10.029 20.643 1.00 23.40 AAAA ATOM 778 CB SER A 108 −11.301 10.108 19.967 1.00 23.85 AAAA ATOM 779 OG SER A 108 −11.292 11.038 18.899 1.00 25.04 AAAA ATOM 780 C SER A 108 −13.121 11.430 21.044 1.00 23.03 AAAA ATOM 781 O SER A 108 −12.592 12.009 21.993 1.00 22.32 AAAA ATOM 782 N GLY A 109 −14.089 11.979 20.310 1.00 21.84 AAAA ATOM 783 CA GLY A 109 −14.583 13.307 20.627 1.00 21.98 AAAA ATOM 784 C GLY A 109 −15.297 13.342 21.972 1.00 20.30 AAAA ATOM 785 O GLY A 109 −14.898 14.088 22.856 1.00 21.37 AAAA ATOM 786 N PRO A 110 −16.369 12.557 22.155 1.00 20.07 AAAA ATOM 787 CD PRO A 110 −16.992 11.637 21.191 1.00 20.80 AAAA ATOM 788 CA PRO A 110 −17.085 12.550 23.436 1.00 19.58 AAAA ATOM 789 CB PRO A 110 −18.232 11.569 23.199 1.00 20.85 AAAA ATOM 790 CG PRO A 110 −18.398 11.548 21.702 1.00 22.43 AAAA ATOM 791 C PRO A 110 −16.136 12.031 24.524 1.00 18.52 AAAA ATOM 792 O PRO A 110 −16.184 12.462 25.675 1.00 19.12 AAAA ATOM 793 N GLY A 111 −15.286 11.086 24.140 1.00 19.12 AAAA ATOM 794 CA GLY A 111 −14.332 10.525 25.087 1.00 18.87 AAAA ATOM 795 C GLY A 111 −13.402 11.601 25.612 1.00 17.97 AAAA ATOM 796 O GLY A 111 −13.208 11.730 26.813 1.00 19.32 AAAA ATOM 797 N GLY A 112 −12.822 12.380 24.704 1.00 18.62 AAAA ATOM 798 CA GLY A 112 −11.925 13.451 25.105 1.00 17.38 AAAA ATOM 799 C GLY A 112 −12.610 14.509 25.957 1.00 17.36 AAAA ATOM 800 O GLY A 112 −12.035 14.997 26.936 1.00 16.49 AAAA ATOM 801 N LEU A 113 −13.837 14.864 25.583 1.00 16.45 AAAA ATOM 802 CA LEU A 113 −14.611 15.866 26.314 1.00 17.35 AAAA ATOM 803 CB LEU A 113 −15.974 16.079 25.640 1.00 17.68 AAAA ATOM 804 CG LEU A 113 −16.735 17.409 25.805 1.00 21.99 AAAA ATOM 805 CD1 LEU A 113 −18.205 17.154 25.511 1.00 20.80 AAAA ATOM 806 CD2 LEU A 113 −16.570 18.007 27.178 1.00 22.94 AAAA ATOM 807 C LEU A 113 −14.836 15.329 27.725 1.00 16.05 AAAA ATOM 808 O LEU A 113 −14.695 16.045 28.711 1.00 16.63 AAAA ATOM 809 N ALA A 114 −15.199 14.056 27.801 1.00 16.59 AAAA ATOM 810 CA ALA A 114 −15.442 13.416 29.087 1.00 15.95 AAAA ATOM 811 CB ALA A 114 −15.859 11.963 28.868 1.00 17.72 AAAA ATOM 812 C ALA A 114 −14.194 13.492 29.968 1.00 15.37 AAAA ATOM 813 O ALA A 114 −14.260 13.952 31.105 1.00 15.94 AAAA ATOM 814 N ALA A 115 −13.053 13.050 29.452 1.00 16.63 AAAA ATOM 815 CA ALA A 115 −11.820 13.098 30.251 1.00 15.65 AAAA ATOM 816 CB ALA A 115 −10.641 12.518 29.450 1.00 15.52 AAAA ATOM 817 C ALA A 115 −11.506 14.530 30.693 1.00 16.10 AAAA ATOM 818 O ALA A 115 −11.141 14.777 31.841 1.00 15.67 AAAA ATOM 819 N TRP A 116 −11.650 15.480 29.778 1.00 16.71 AAAA ATOM 820 CA TRP A 116 −11.380 16.873 30.100 1.00 17.31 AAAA ATOM 821 CB TRP A 116 −11.542 17.723 28.835 1.00 18.91 AAAA ATOM 822 CG TRP A 116 −11.172 19.155 29.003 1.00 21.69 AAAA ATOM 823 CD2 TRP A 116 −12.008 20.277 28.740 1.00 23.65 AAAA ATOM 824 CE2 TRP A 116 −11.262 21.438 29.048 1.00 25.14 AAAA ATOM 825 CE3 TRP A 116 −13.321 20.418 28.268 1.00 26.49 AAAA ATOM 826 CD1 TRP A 116 −9.979 19.658 29.447 1.00 23.00 AAAA ATOM 827 NE1 TRP A 116 −10.025 21.032 29.479 1.00 24.96 AAAA ATOM 828 CZ2 TRP A 116 −11.785 22.724 28.902 1.00 26.16 AAAA ATOM 829 CZ3 TRP A 116 −13.842 21.702 28.122 1.00 26.44 AAAA ATOM 830 CH2 TRP A 116 −13.072 22.834 28.439 1.00 25.35 AAAA ATOM 831 C TRP A 116 −12.292 17.377 31.233 1.00 16.50 AAAA ATOM 832 O TRP A 116 −11.835 18.080 32.137 1.00 16.03 AAAA ATOM 833 N SER A 117 −13.565 16.990 31.200 1.00 16.73 AAAA ATOM 834 CA SER A 117 −14.528 17.399 32.229 1.00 17.06 AAAA ATOM 835 CB SER A 117 −15.961 17.116 31.762 1.00 16.18 AAAA ATOM 836 OG SER A 117 −16.270 15.731 31.743 1.00 18.31 AAAA ATOM 837 C SER A 117 −14.289 16.720 33.586 1.00 18.05 AAAA ATOM 838 O SER A 117 −14.837 17.147 34.605 1.00 17.79 AAAA ATOM 839 N LEU A 118 −13.466 15.678 33.594 1.00 18.13 AAAA ATOM 840 CA LEU A 118 −13.146 14.950 34.827 1.00 19.26 AAAA ATOM 841 CB LEU A 118 −13.262 13.441 34.587 1.00 18.09 AAAA ATOM 842 CG LEU A 118 −14.686 12.932 34.353 1.00 20.04 AAAA ATOM 843 CD1 LEU A 118 −14.659 11.484 33.869 1.00 20.30 AAAA ATOM 844 CD2 LEU A 118 −15.480 13.064 35.646 1.00 20.40 AAAA ATOM 845 C LEU A 118 −11.736 15.283 35.305 1.00 20.78 AAAA ATOM 846 O LEU A 118 −11.267 14.763 36.321 1.00 20.64 AAAA ATOM 847 N GLY A 119 −11.057 16.152 34.566 1.00 21.27 AAAA ATOM 848 CA GLY A 119 −9.706 16.537 34.943 1.00 21.97 AAAA ATOM 849 C GLY A 119 −8.648 15.519 34.550 1.00 21.55 AAAA ATOM 850 O GLY A 119 −7.515 15.582 35.034 1.00 21.92 AAAA ATOM 851 N ILE A 120 −9.009 14.584 33.678 1.00 20.43 AAAA ATOM 852 CA ILE A 120 −8.082 13.548 33.214 1.00 21.09 AAAA ATOM 853 CB ILE A 120 −8.853 12.270 32.836 1.00 20.95 AAAA ATOM 854 CG2 ILE A 120 −7.902 11.226 32.275 1.00 22.20 AAAA ATOM 855 CG1 ILE A 120 −9.624 11.748 34.051 1.00 22.05 AAAA ATOM 856 CD1 ILE A 120 −10.688 10.709 33.689 1.00 21.95 AAAA ATOM 857 C ILE A 120 −7.358 14.088 31.978 1.00 20.81 AAAA ATOM 858 O ILE A 120 −8.001 14.465 31.004 1.00 21.35 AAAA ATOM 859 N PRO A 121 −6.013 14.131 31.999 1.00 20.67 AAAA ATOM 860 CD PRO A 121 −5.052 13.722 33.040 1.00 20.88 AAAA ATOM 861 CA PRO A 121 −5.320 14.658 30.819 1.00 20.52 AAAA ATOM 862 CB PRO A 121 −3.842 14.649 31.237 1.00 21.37 AAAA ATOM 863 CG PRO A 121 −3.777 13.532 32.240 1.00 22.04 AAAA ATOM 864 C PRO A 121 −5.580 13.893 29.536 1.00 19.38 AAAA ATOM 865 O PRO A 121 −5.717 12.671 29.538 1.00 18.17 AAAA ATOM 866 N VAL A 122 −5.647 14.645 28.442 1.00 20.01 AAAA ATOM 867 CA VAL A 122 −5.903 14.102 27.120 1.00 19.76 AAAA ATOM 868 CB VAL A 122 −7.047 14.866 26.421 1.00 18.63 AAAA ATOM 869 CG1 VAL A 122 −7.286 14.281 25.033 1.00 20.46 AAAA ATOM 870 CG2 VAL A 122 −8.320 14.790 27.264 1.00 20.31 AAAA ATOM 871 C VAL A 122 −4.672 14.205 26.223 1.00 19.39 AAAA ATOM 872 O VAL A 122 −4.096 15.282 26.069 1.00 19.66 AAAA ATOM 873 N VAL A 123 −4.284 13.079 25.634 1.00 19.86 AAAA ATOM 874 CA VAL A 123 −3.134 13.029 24.734 1.00 20.22 AAAA ATOM 875 CB VAL A 123 −2.086 11.982 25.200 1.00 20.59 AAAA ATOM 876 CG1 VAL A 123 −0.898 11.957 24.226 1.00 20.51 AAAA ATOM 877 CG2 VAL A 123 −1.602 12.317 26.606 1.00 17.21 AAAA ATOM 878 C VAL A 123 −3.684 12.600 23.381 1.00 21.06 AAAA ATOM 879 O VAL A 123 −4.482 11.666 23.300 1.00 22.10 AAAA ATOM 880 N LEU A 124 −3.269 13.284 22.325 1.00 21.08 AAAA ATOM 881 CA LEU A 124 −3.746 12.952 20.989 1.00 21.68 AAAA ATOM 882 CB LEU A 124 −4.463 14.149 20.366 1.00 21.81 AAAA ATOM 883 CG LEU A 124 −5.629 14.805 21.105 1.00 21.93 AAAA ATOM 884 CD1 LEU A 124 −6.133 15.980 20.268 1.00 22.15 AAAA ATOM 885 CD2 LEU A 124 −6.737 13.787 21.337 1.00 21.49 AAAA ATOM 886 C LEU A 124 −2.628 12.558 20.038 1.00 21.67 AAAA ATOM 887 O LEU A 124 −1.493 13.011 20.170 1.00 22.39 AAAA ATOM 888 N HIS A 125 −2.964 11.713 19.075 1.00 22.63 AAAA ATOM 889 CA HIS A 125 −2.014 11.336 18.036 1.00 24.74 AAAA ATOM 890 CB HIS A 125 −1.429 9.939 18.244 1.00 24.62 AAAA ATOM 891 CG HIS A 125 −0.471 9.540 17.162 1.00 27.30 AAAA ATOM 892 CD2 HIS A 125 −0.629 8.744 16.079 1.00 27.23 AAAA ATOM 893 ND1 HIS A 125 0.806 10.057 17.072 1.00 29.96 AAAA ATOM 894 CE1 HIS A 125 1.391 9.597 15.979 1.00 27.40 AAAA ATOM 895 NE2 HIS A 125 0.541 8.799 15.358 1.00 28.94 AAAA ATOM 896 C HIS A 125 −2.763 11.364 16.705 1.00 24.38 AAAA ATOM 897 O HIS A 125 −3.813 10.741 16.565 1.00 23.93 AAAA ATOM 898 N GLU A 126 −2.233 12.111 15.744 1.00 24.36 AAAA ATOM 899 CA GLU A 126 −2.836 12.199 14.420 1.00 26.31 AAAA ATOM 900 CB GLU A 126 −2.992 13.664 14.005 1.00 25.81 AAAA ATOM 901 CG GLU A 126 −3.465 13.861 12.567 1.00 26.62 AAAA ATOM 902 CD GLU A 126 −4.795 13.196 12.288 1.00 27.69 AAAA ATOM 903 OE1 GLU A 126 −5.785 13.544 12.965 1.00 27.90 AAAA ATOM 904 OE2 GLU A 126 −4.855 12.326 11.391 1.00 27.53 AAAA ATOM 905 C GLU A 126 −1.901 11.472 13.456 1.00 27.49 AAAA ATOM 906 O GLU A 126 −0.727 11.819 13.349 1.00 27.87 AAAA ATOM 907 N GLN A 127 −2.423 10.463 12.765 1.00 28.80 AAAA ATOM 908 CA GLN A 127 −1.617 9.682 11.834 1.00 30.09 AAAA ATOM 909 CB GLN A 127 −2.192 8.264 11.688 1.00 28.89 AAAA ATOM 910 CG GLN A 127 −2.184 7.421 12.958 1.00 28.94 AAAA ATOM 911 CD GLN A 127 −3.456 7.578 13.775 1.00 29.34 AAAA ATOM 912 OE1 GLN A 127 −4.543 7.207 13.329 1.00 29.36 AAAA ATOM 913 NE2 GLN A 127 −3.326 8.131 14.973 1.00 28.70 AAAA ATOM 914 C GLN A 127 −1.455 10.277 10.438 1.00 30.92 AAAA ATOM 915 O GLN A 127 −0.428 10.068 9.794 1.00 31.21 AAAA ATOM 916 N ASN A 128 −2.448 11.038 9.986 1.00 32.48 AAAA ATOM 917 CA ASN A 128 −2.434 11.596 8.634 1.00 33.12 AAAA ATOM 918 CB ASN A 128 −3.864 11.589 8.083 1.00 32.20 AAAA ATOM 919 CG ASN A 128 −4.606 10.312 8.424 1.00 33.05 AAAA ATOM 920 OD1 ASN A 128 −5.296 10.236 9.445 1.00 33.34 AAAA ATOM 921 ND2 ASN A 128 −4.454 9.292 7.584 1.00 31.22 AAAA ATOM 922 C ASN A 128 −1.809 12.971 8.394 1.00 33.60 AAAA ATOM 923 O ASN A 128 −1.571 13.744 9.327 1.00 34.03 AAAA ATOM 924 N GLY A 129 −1.550 13.256 7.117 1.00 33.69 AAAA ATOM 925 CA GLY A 129 −0.959 14.524 6.718 1.00 33.68 AAAA ATOM 926 C GLY A 129 −1.903 15.682 6.972 1.00 33.41 AAAA ATOM 927 O GLY A 129 −1.482 16.834 7.057 1.00 32.92 AAAA ATOM 928 N ILE A 130 −3.192 15.374 7.070 1.00 33.49 AAAA ATOM 929 CA ILE A 130 −4.205 16.383 7.361 1.00 33.06 AAAA ATOM 930 CB ILE A 130 −5.204 16.570 6.206 1.00 33.49 AAAA ATOM 931 CG2 ILE A 130 −4.548 17.358 5.083 1.00 35.66 AAAA ATOM 932 CG1 ILE A 130 −5.736 15.209 5.751 1.00 34.45 AAAA ATOM 933 CD1 ILE A 130 −6.775 15.279 4.665 1.00 35.68 AAAA ATOM 934 C ILE A 130 −4.964 15.892 8.584 1.00 32.19 AAAA ATOM 935 O ILE A 130 −5.379 14.733 8.644 1.00 32.07 AAAA ATOM 936 N ALA A 131 −5.135 16.771 9.561 1.00 31.26 AAAA ATOM 937 CA ALA A 131 −5.832 16.404 10.788 1.00 30.63 AAAA ATOM 938 CB ALA A 131 −5.735 17.547 11.800 1.00 30.70 AAAA ATOM 939 C ALA A 131 −7.292 16.038 10.556 1.00 30.27 AAAA ATOM 940 O ALA A 131 −7.992 16.682 9.774 1.00 30.54 AAAA ATOM 941 N GLY A 132 −7.743 14.987 11.232 1.00 29.03 AAAA ATOM 942 CA GLY A 132 −9.131 14.587 11.119 1.00 27.98 AAAA ATOM 943 C GLY A 132 −9.902 15.678 11.837 1.00 26.80 AAAA ATOM 944 O GLY A 132 −9.326 16.387 12.660 1.00 25.68 AAAA ATOM 945 N LEU A 133 −11.188 15.827 11.543 1.00 26.51 AAAA ATOM 946 CA LEU A 133 −11.973 16.882 12.186 1.00 26.70 AAAA ATOM 947 CB LEU A 133 −13.363 16.967 11.538 1.00 28.16 AAAA ATOM 948 CG LEU A 133 −14.275 18.138 11.936 1.00 28.52 AAAA ATOM 949 CD1 LEU A 133 −14.889 17.874 13.280 1.00 32.18 AAAA ATOM 950 CD2 LEU A 133 −13.486 19.436 11.960 1.00 30.27 AAAA ATOM 951 C LEU A 133 −12.097 16.713 13.703 1.00 25.88 AAAA ATOM 952 O LEU A 133 −12.063 17.700 14.444 1.00 26.12 AAAA ATOM 953 N THR A 134 −12.240 15.475 14.169 1.00 24.18 AAAA ATOM 954 CA THR A 134 −12.353 15.230 15.608 1.00 23.78 AAAA ATOM 955 CB THR A 134 −12.605 13.729 15.922 1.00 23.18 AAAA ATOM 956 OG1 THR A 134 −13.814 13.300 15.285 1.00 23.74 AAAA ATOM 957 CG2 THR A 134 −12.751 13.511 17.433 1.00 23.66 AAAA ATOM 958 C THR A 134 −11.071 15.671 16.315 1.00 22.68 AAAA ATOM 959 O THR A 134 −11.116 16.368 17.328 1.00 21.38 AAAA ATOM 960 N ASN A 135 −9.927 15.267 15.771 1.00 23.98 AAAA ATOM 961 CA ASN A 135 −8.636 15.623 16.358 1.00 24.64 AAAA ATOM 962 CB ASN A 135 −7.488 14.936 15.597 1.00 24.49 AAAA ATOM 963 CG ASN A 135 −7.020 13.638 16.264 1.00 25.25 AAAA ATOM 964 OD1 ASN A 135 −6.267 12.856 15.668 1.00 25.70 AAAA ATOM 965 ND2 ASN A 135 −7.445 13.415 17.504 1.00 22.51 AAAA ATOM 966 C ASN A 135 −8.421 17.135 16.349 1.00 25.19 AAAA ATOM 967 O ASN A 135 −7.890 17.702 17.301 1.00 24.79 AAAA ATOM 968 N LYS A 136 −8.839 17.792 15.274 1.00 26.78 AAAA ATOM 969 CA LYS A 136 −8.661 19.234 15.177 1.00 28.71 AAAA ATOM 970 CB LYS A 136 −9.165 19.743 13.828 1.00 30.84 AAAA ATOM 971 CG LYS A 136 −8.816 21.195 13.563 1.00 34.68 AAAA ATOM 972 CD LYS A 136 −9.206 21.596 12.148 1.00 36.19 AAAA ATOM 973 CE LYS A 136 −8.810 23.033 11.846 1.00 37.78 AAAA ATOM 974 NZ LYS A 136 −9.124 23.414 10.432 1.00 40.33 AAAA ATOM 975 C LYS A 136 −9.370 19.981 16.304 1.00 28.66 AAAA ATOM 976 O LYS A 136 −8.803 20.900 16.902 1.00 28.47 AAAA ATOM 977 N TRP A 137 −10.606 19.589 16.596 1.00 28.05 AAAA ATOM 978 CA TRP A 137 −11.363 20.243 17.656 1.00 28.85 AAAA ATOM 979 CB TRP A 137 −12.855 19.921 17.516 1.00 31.86 AAAA ATOM 980 CG TRP A 137 −13.485 20.502 16.282 1.00 34.71 AAAA ATOM 981 CD2 TRP A 137 −14.788 20.206 15.755 1.00 36.70 AAAA ATOM 982 CE2 TRP A 137 −14.982 21.036 14.630 1.00 37.21 AAAA ATOM 983 CE3 TRP A 137 −15.811 19.321 16.130 1.00 38.46 AAAA ATOM 984 CD1 TRP A 137 −12.959 21.466 15.471 1.00 36.22 AAAA ATOM 985 NE1 TRP A 137 −13.851 21.794 14.480 1.00 36.96 AAAA ATOM 986 CZ2 TRP A 137 −16.160 21.010 13.869 1.00 38.57 AAAA ATOM 987 CZ3 TRP A 137 −16.986 19.295 15.373 1.00 39.12 AAAA ATOM 988 CH2 TRP A 137 −17.148 20.136 14.255 1.00 39.31 AAAA ATOM 989 C TRP A 137 −10.868 19.803 19.029 1.00 28.01 AAAA ATOM 990 O TRP A 137 −10.763 20.605 19.955 1.00 27.04 AAAA ATOM 991 N LEU A 138 −10.548 18.520 19.143 1.00 27.31 AAAA ATOM 992 CA LEU A 138 −10.072 17.943 20.393 1.00 26.35 AAAA ATOM 993 CB LEU A 138 −9.879 16.444 20.174 1.00 27.79 AAAA ATOM 994 CG LEU A 138 −10.054 15.384 21.262 1.00 30.24 AAAA ATOM 995 CD1 LEU A 138 −11.263 15.650 22.142 1.00 29.67 AAAA ATOM 996 CD2 LEU A 138 −10.178 14.036 20.562 1.00 30.06 AAAA ATOM 997 C LEU A 138 −8.772 18.609 20.834 1.00 25.34 AAAA ATOM 998 O LEU A 138 −8.532 18.814 22.030 1.00 23.81 AAAA ATOM 999 N ALA A 139 −7.931 18.953 19.865 1.00 26.03 AAAA ATOM 1000 CA ALA A 139 −6.657 19.595 20.160 1.00 26.05 AAAA ATOM 1001 CB ALA A 139 −5.918 19.934 18.858 1.00 26.98 AAAA ATOM 1002 C ALA A 139 −6.847 20.858 21.002 1.00 26.86 AAAA ATOM 1003 O ALA A 139 −5.929 21.286 21.697 1.00 26.11 AAAA ATOM 1004 N LYS A 140 −8.044 21.439 20.952 1.00 26.32 AAAA ATOM 1005 CA LYS A 140 −8.329 22.649 21.716 1.00 26.90 AAAA ATOM 1006 CB LYS A 140 −9.644 23.276 21.238 1.00 29.14 AAAA ATOM 1007 CG LYS A 140 −9.665 23.595 19.749 1.00 31.62 AAAA ATOM 1008 CD LYS A 140 −8.523 24.513 19.364 1.00 35.02 AAAA ATOM 1009 CE LYS A 140 −8.811 25.975 19.704 1.00 37.44 AAAA ATOM 1010 NZ LYS A 140 −9.865 26.555 18.812 1.00 40.43 AAAA ATOM 1011 C LYS A 140 −8.395 22.414 23.230 1.00 25.59 AAAA ATOM 1012 O LYS A 140 −8.333 23.361 24.004 1.00 24.94 AAAA ATOM 1013 N ILE A 141 −8.526 21.159 23.649 1.00 24.13 AAAA ATOM 1014 CA ILE A 141 −8.587 20.844 25.075 1.00 23.31 AAAA ATOM 1015 CB ILE A 141 −9.971 20.270 25.477 1.00 22.85 AAAA ATOM 1016 CG2 ILE A 141 −11.046 21.355 25.372 1.00 23.88 AAAA ATOM 1017 CG1 ILE A 141 −10.313 19.071 24.595 1.00 23.34 AAAA ATOM 1018 CD1 ILE A 141 −11.574 18.339 25.012 1.00 25.61 AAAA ATOM 1019 C ILE A 141 −7.524 19.822 25.482 1.00 23.06 AAAA ATOM 1020 O ILE A 141 −7.427 19.450 26.655 1.00 22.52 AAAA ATOM 1021 N ALA A 142 −6.724 19.375 24.520 1.00 21.80 AAAA ATOM 1022 CA ALA A 142 −5.695 18.379 24.803 1.00 21.97 AAAA ATOM 1023 CB ALA A 142 −5.231 17.739 23.495 1.00 20.41 AAAA ATOM 1024 C ALA A 142 −4.491 18.924 25.580 1.00 21.11 AAAA ATOM 1025 O ALA A 142 −4.132 20.094 25.465 1.00 22.76 AAAA ATOM 1026 N THR A 143 −3.887 18.056 26.384 1.00 21.92 AAAA ATOM 1027 CA THR A 143 −2.707 18.391 27.178 1.00 22.64 AAAA ATOM 1028 CB THR A 143 −2.598 17.450 28.400 1.00 23.91 AAAA ATOM 1029 OG1 THR A 143 −3.751 17.635 29.232 1.00 25.42 AAAA ATOM 1030 CG2 THR A 143 −1.329 17.735 29.209 1.00 24.48 AAAA ATOM 1031 C THR A 143 −1.454 18.235 26.312 1.00 22.79 AAAA ATOM 1032 O THR A 143 −0.444 18.910 26.517 1.00 23.30 AAAA ATOM 1033 N LYS A 144 −1.525 17.341 25.335 1.00 23.20 AAAA ATOM 1034 CA LYS A 144 −0.398 17.106 24.440 1.00 25.09 AAAA ATOM 1035 CB LYS A 144 0.565 16.083 25.049 1.00 25.01 AAAA ATOM 1036 CG LYS A 144 1.706 15.658 24.129 1.00 28.28 AAAA ATOM 1037 CD LYS A 144 2.604 16.838 23.747 1.00 27.48 AAAA ATOM 1038 CE LYS A 144 3.818 16.373 22.946 1.00 29.11 AAAA ATOM 1039 NZ LYS A 144 4.722 17.507 22.587 1.00 28.97 AAAA ATOM 1040 C LYS A 144 −0.896 16.595 23.102 1.00 24.77 AAAA ATOM 1041 O LYS A 144 −1.688 15.660 23.039 1.00 24.45 AAAA ATOM 1042 N VAL A 145 −0.432 17.218 22.030 1.00 24.92 AAAA ATOM 1043 CA VAL A 145 −0.830 16.793 20.701 1.00 25.14 AAAA ATOM 1044 CB VAL A 145 −1.510 17.938 19.919 1.00 24.18 AAAA ATOM 1045 CG1 VAL A 145 −2.023 17.418 18.591 1.00 24.71 AAAA ATOM 1046 CG2 VAL A 145 −2.658 18.528 20.740 1.00 25.82 AAAA ATOM 1047 C VAL A 145 0.420 16.356 19.950 1.00 25.49 AAAA ATOM 1048 O VAL A 145 1.449 17.034 19.995 1.00 25.76 AAAA ATOM 1049 N MET A 146 0.324 15.208 19.289 1.00 26.18 AAAA ATOM 1050 CA MET A 146 1.421 14.654 18.503 1.00 26.41 AAAA ATOM 1051 CB MET A 146 2.000 13.396 19.172 1.00 26.85 AAAA ATOM 1052 CG MET A 146 2.826 13.653 20.430 1.00 25.85 AAAA ATOM 1053 SD MET A 146 3.306 12.116 21.269 1.00 28.45 AAAA ATOM 1054 CE MET A 146 1.827 11.741 22.217 1.00 26.47 AAAA ATOM 1055 C MET A 146 0.860 14.293 17.131 1.00 27.20 AAAA ATOM 1056 O MET A 146 −0.311 13.934 16.998 1.00 25.68 AAAA ATOM 1057 N GLN A 147 1.701 14.395 16.111 1.00 28.03 AAAA ATOM 1058 CA GLN A 147 1.294 14.091 14.748 1.00 28.39 AAAA ATOM 1059 CB GLN A 147 1.067 15.388 13.979 1.00 28.65 AAAA ATOM 1060 CG GLN A 147 2.203 16.371 14.142 1.00 30.13 AAAA ATOM 1061 CD GLN A 147 2.006 17.653 13.360 1.00 29.84 AAAA ATOM 1062 OE1 GLN A 147 2.730 18.629 13.565 1.00 32.18 AAAA ATOM 1063 NE2 GLN A 147 1.036 17.657 12.453 1.00 29.40 AAAA ATOM 1064 C GLN A 147 2.394 13.274 14.085 1.00 29.45 AAAA ATOM 1065 O GLN A 147 3.570 13.420 14.424 1.00 29.21 AAAA ATOM 1066 N ALA A 148 2.010 12.412 13.150 1.00 29.90 AAAA ATOM 1067 CA ALA A 148 2.975 11.563 12.461 1.00 31.39 AAAA ATOM 1068 CB ALA A 148 2.254 10.468 11.690 1.00 30.97 AAAA ATOM 1069 C ALA A 148 3.846 12.373 11.514 1.00 32.66 AAAA ATOM 1070 O ALA A 148 5.071 12.231 11.517 1.00 32.76 AAAA ATOM 1071 N PHE A 149 3.205 13.220 10.712 1.00 33.44 AAAA ATOM 1072 CA PHE A 149 3.903 14.059 9.744 1.00 35.09 AAAA ATOM 1073 CB PHE A 149 3.367 13.814 8.332 1.00 34.59 AAAA ATOM 1074 CG PHE A 149 3.200 12.367 7.985 1.00 35.35 AAAA ATOM 1075 CD1 PHE A 149 1.935 11.789 7.958 1.00 34.17 AAAA ATOM 1076 CD2 PHE A 149 4.304 11.579 7.685 1.00 34.88 AAAA ATOM 1077 CE1 PHE A 149 1.771 10.448 7.637 1.00 34.20 AAAA ATOM 1078 CE2 PHE A 149 4.148 10.236 7.364 1.00 36.09 AAAA ATOM 1079 CZ PHE A 149 2.878 9.670 7.340 1.00 35.09 AAAA ATOM 1080 C PHE A 149 3.719 15.536 10.056 1.00 36.17 AAAA ATOM 1081 O PHE A 149 2.697 15.939 10.606 1.00 37.06 AAAA ATOM 1082 N PRO A 150 4.709 16.370 9.704 1.00 37.23 AAAA ATOM 1083 CD PRO A 150 6.002 16.078 9.056 1.00 37.75 AAAA ATOM 1084 CA PRO A 150 4.569 17.803 9.975 1.00 38.03 AAAA ATOM 1085 CB PRO A 150 5.967 18.341 9.682 1.00 38.69 AAAA ATOM 1086 CG PRO A 150 6.432 17.448 8.569 1.00 38.52 AAAA ATOM 1087 C PRO A 150 3.510 18.369 9.028 1.00 38.18 AAAA ATOM 1088 O PRO A 150 3.355 17.878 7.912 1.00 38.42 AAAA ATOM 1089 N GLY A 151 2.763 19.374 9.475 1.00 38.74 AAAA ATOM 1090 CA GLY A 151 1.749 19.952 8.609 1.00 38.66 AAAA ATOM 1091 C GLY A 151 0.300 19.705 8.996 1.00 38.69 AAAA ATOM 1092 O GLY A 151 −0.571 20.502 8.645 1.00 38.08 AAAA ATOM 1093 N ALA A 152 0.024 18.602 9.689 1.00 38.70 AAAA ATOM 1094 CA ALA A 152 −1.343 18.311 10.112 1.00 38.90 AAAA ATOM 1095 CB ALA A 152 −1.402 16.980 10.859 1.00 38.46 AAAA ATOM 1096 C ALA A 152 −1.729 19.461 11.032 1.00 39.30 AAAA ATOM 1097 O ALA A 152 −2.753 20.114 10.838 1.00 40.05 AAAA ATOM 1098 N PHE A 153 −0.887 19.700 12.031 1.00 39.42 AAAA ATOM 1099 CA PHE A 153 −1.084 20.795 12.971 1.00 39.90 AAAA ATOM 1100 CB PHE A 153 −1.209 20.286 14.409 1.00 39.04 AAAA ATOM 1101 CG PHE A 153 −2.478 19.535 14.685 1.00 38.06 AAAA ATOM 1102 CD1 PHE A 153 −2.571 18.175 14.419 1.00 36.71 AAAA ATOM 1103 CD2 PHE A 153 −3.582 20.190 15.228 1.00 37.52 AAAA ATOM 1104 CE1 PHE A 153 −3.747 17.475 14.692 1.00 36.39 AAAA ATOM 1105 CE2 PHE A 153 −4.761 19.500 15.502 1.00 36.08 AAAA ATOM 1106 CZ PHE A 153 −4.842 18.140 15.235 1.00 36.20 AAAA ATOM 1107 C PHE A 153 0.143 21.696 12.865 1.00 40.75 AAAA ATOM 1108 O PHE A 153 1.238 21.228 12.543 1.00 41.03 AAAA ATOM 1109 N PRO A 154 −0.026 23.001 13.128 1.00 41.05 AAAA ATOM 1110 CD PRO A 154 −1.328 23.667 13.304 1.00 41.17 AAAA ATOM 1111 CA PRO A 154 1.052 23.992 13.068 1.00 41.57 AAAA ATOM 1112 CB PRO A 154 0.339 25.292 13.428 1.00 41.69 AAAA ATOM 1113 CG PRO A 154 −1.024 25.081 12.876 1.00 41.76 AAAA ATOM 1114 C PRO A 154 2.260 23.744 13.975 1.00 42.12 AAAA ATOM 1115 O PRO A 154 3.400 23.833 13.515 1.00 43.15 AAAA ATOM 1116 N ASN A 155 2.023 23.432 15.249 1.00 41.75 AAAA ATOM 1117 CA ASN A 155 3.135 23.230 16.180 1.00 41.57 AAAA ATOM 1118 CB ASN A 155 3.180 24.389 17.179 1.00 44.02 AAAA ATOM 1119 CG ASN A 155 2.961 25.736 16.522 1.00 45.69 AAAA ATOM 1120 OD1 ASN A 155 1.862 26.045 16.058 1.00 47.64 AAAA ATOM 1121 ND2 ASN A 155 4.010 26.545 16.475 1.00 47.43 AAAA ATOM 1122 C ASN A 155 3.193 21.921 16.970 1.00 40.83 AAAA ATOM 1123 O ASN A 155 3.973 21.814 17.917 1.00 41.17 AAAA ATOM 1124 N ALA A 156 2.390 20.929 16.601 1.00 38.83 AAAA ATOM 1125 CA ALA A 156 2.400 19.658 17.326 1.00 37.19 AAAA ATOM 1126 CB ALA A 156 1.203 18.811 16.909 1.00 36.03 AAAA ATOM 1127 C ALA A 156 3.698 18.882 17.090 1.00 35.95 AAAA ATOM 1128 O ALA A 156 4.206 18.834 15.971 1.00 35.55 AAAA ATOM 1129 N GLU A 157 4.233 18.275 18.146 1.00 35.08 AAAA ATOM 1130 CA GLU A 157 5.464 17.505 18.022 1.00 33.77 AAAA ATOM 1131 CB GLU A 157 5.848 16.881 19.373 1.00 34.33 AAAA ATOM 1132 CG GLU A 157 7.175 16.124 19.352 1.00 34.59 AAAA ATOM 1133 CD GLU A 157 7.487 15.430 20.670 1.00 35.45 AAAA ATOM 1134 OE1 GLU A 157 8.517 14.729 20.746 1.00 34.09 AAAA ATOM 1135 OE2 GLU A 157 6.705 15.582 21.631 1.00 36.21 AAAA ATOM 1136 C GLU A 157 5.282 16.405 16.970 1.00 32.70 AAAA ATOM 1137 O GLU A 157 4.262 15.709 16.952 1.00 31.88 AAAA ATOM 1138 N VAL A 158 6.268 16.265 16.088 1.00 31.00 AAAA ATOM 1139 CA VAL A 158 6.230 15.255 15.032 1.00 30.25 AAAA ATOM 1140 CB VAL A 158 6.926 15.768 13.751 1.00 30.33 AAAA ATOM 1141 CG1 VAL A 158 7.013 14.653 12.719 1.00 29.98 AAAA ATOM 1142 CG2 VAL A 158 6.147 16.953 13.181 1.00 30.15 AAAA ATOM 1143 C VAL A 158 6.937 13.998 15.529 1.00 29.69 AAAA ATOM 1144 O VAL A 158 8.142 14.020 15.798 1.00 29.80 AAAA ATOM 1145 N VAL A 159 6.182 12.909 15.645 1.00 28.61 AAAA ATOM 1146 CA VAL A 159 6.715 11.647 16.149 1.00 29.00 AAAA ATOM 1147 CB VAL A 159 6.019 11.250 17.469 1.00 28.75 AAAA ATOM 1148 CG1 VAL A 159 6.129 12.384 18.482 1.00 28.06 AAAA ATOM 1149 CG2 VAL A 159 4.552 10.921 17.197 1.00 28.06 AAAA ATOM 1150 C VAL A 159 6.581 10.469 15.186 1.00 29.32 AAAA ATOM 1151 O VAL A 159 7.066 9.376 15.479 1.00 29.89 AAAA ATOM 1152 N GLY A 160 5.915 10.688 14.054 1.00 30.03 AAAA ATOM 1153 CA GLY A 160 5.727 9.628 13.075 1.00 29.63 AAAA ATOM 1154 C GLY A 160 4.678 8.608 13.483 1.00 29.61 AAAA ATOM 1155 O GLY A 160 3.917 8.849 14.416 1.00 29.30 AAAA ATOM 1156 N ASN A 161 4.635 7.475 12.782 1.00 29.30 AAAA ATOM 1157 CA ASN A 161 3.677 6.401 13.074 1.00 29.78 AAAA ATOM 1158 CB ASN A 161 2.800 6.097 11.858 1.00 30.70 AAAA ATOM 1159 CG ASN A 161 1.755 7.154 11.609 1.00 32.16 AAAA ATOM 1160 OD1 ASN A 161 0.951 7.461 12.492 1.00 31.78 AAAA ATOM 1161 ND2 ASN A 161 1.750 7.711 10.400 1.00 30.88 AAAA ATOM 1162 C ASN A 161 4.344 5.089 13.462 1.00 29.50 AAAA ATOM 1163 O ASN A 161 5.471 4.810 13.058 1.00 29.61 AAAA ATOM 1164 N PRO A 162 3.648 4.263 14.251 1.00 29.59 AAAA ATOM 1165 CD PRO A 162 2.441 4.571 15.039 1.00 29.95 AAAA ATOM 1166 CA PRO A 162 4.219 2.977 14.650 1.00 29.65 AAAA ATOM 1167 CB PRO A 162 3.143 2.389 15.553 1.00 29.79 AAAA ATOM 1168 CG PRO A 162 2.559 3.608 16.200 1.00 30.38 AAAA ATOM 1169 C PRO A 162 4.423 2.135 13.389 1.00 30.13 AAAA ATOM 1170 O PRO A 162 3.535 2.063 12.531 1.00 28.48 AAAA ATOM 1171 N VAL A 163 5.590 1.508 13.287 1.00 29.92 AAAA ATOM 1172 CA VAL A 163 5.935 0.664 12.149 1.00 29.89 AAAA ATOM 1173 CB VAL A 163 7.182 1.224 11.417 1.00 31.04 AAAA ATOM 1174 CG1 VAL A 163 7.571 0.308 10.260 1.00 30.44 AAAA ATOM 1175 CG2 VAL A 163 6.902 2.631 10.914 1.00 29.10 AAAA ATOM 1176 C VAL A 163 6.258 −0.744 12.652 1.00 31.06 AAAA ATOM 1177 O VAL A 163 6.884 −0.892 13.706 1.00 29.66 AAAA ATOM 1178 N ARG A 164 5.820 −1.773 11.927 1.00 31.83 AAAA ATOM 1179 CA ARG A 164 6.124 −3.142 12.339 1.00 34.34 AAAA ATOM 1180 CB ARG A 164 5.533 −4.167 11.354 1.00 36.31 AAAA ATOM 1181 CG ARG A 164 5.704 −3.841 9.876 1.00 39.86 AAAA ATOM 1182 CD ARG A 164 4.855 −4.770 8.997 1.00 41.13 AAAA ATOM 1183 NE ARG A 164 5.368 −6.140 8.946 1.00 43.44 AAAA ATOM 1184 CZ ARG A 164 4.765 −7.145 8.311 1.00 44.08 AAAA ATOM 1185 NH1 ARG A 164 3.619 −6.940 7.671 1.00 44.91 AAAA ATOM 1186 NH2 ARG A 164 5.308 −8.355 8.308 1.00 44.44 AAAA ATOM 1187 C ARG A 164 7.649 −3.248 12.419 1.00 34.72 AAAA ATOM 1188 O ARG A 164 8.364 −2.769 11.537 1.00 33.63 AAAA ATOM 1189 N THR A 165 8.138 −3.855 13.496 1.00 34.72 AAAA ATOM 1190 CA THR A 165 9.567 −3.969 13.730 1.00 34.94 AAAA ATOM 1191 CB THR A 165 9.839 −4.437 15.177 1.00 35.90 AAAA ATOM 1192 OG1 THR A 165 9.008 −5.563 15.488 1.00 36.96 AAAA ATOM 1193 CG2 THR A 165 9.530 −3.313 16.149 1.00 35.88 AAAA ATOM 1194 C THR A 165 10.373 −4.814 12.749 1.00 34.61 AAAA ATOM 1195 O THR A 165 11.577 −4.603 12.608 1.00 34.56 AAAA ATOM 1196 N ASP A 166 9.739 −5.765 12.068 1.00 34.66 AAAA ATOM 1197 CA ASP A 166 10.492 −6.558 11.103 1.00 34.85 AAAA ATOM 1198 CB ASP A 166 9.697 −7.784 10.642 1.00 36.47 AAAA ATOM 1199 CG ASP A 166 8.341 −7.430 10.089 1.00 37.65 AAAA ATOM 1200 OD1 ASP A 166 7.566 −8.365 9.804 1.00 41.03 AAAA ATOM 1201 OD2 ASP A 166 8.048 −6.227 9.937 1.00 39.97 AAAA ATOM 1202 C ASP A 166 10.862 −5.667 9.917 1.00 33.70 AAAA ATOM 1203 O ASP A 166 11.846 −5.925 9.224 1.00 34.04 AAAA ATOM 1204 N VAL A 167 10.081 −4.610 9.694 1.00 31.98 AAAA ATOM 1205 CA VAL A 167 10.366 −3.667 8.611 1.00 31.43 AAAA ATOM 1206 CB VAL A 167 9.096 −2.888 8.170 1.00 31.53 AAAA ATOM 1207 CG1 VAL A 167 9.485 −1.738 7.248 1.00 30.83 AAAA ATOM 1208 CG2 VAL A 167 8.120 −3.825 7.458 1.00 31.61 AAAA ATOM 1209 C VAL A 167 11.400 −2.657 9.108 1.00 31.23 AAAA ATOM 1210 O VAL A 167 12.320 −2.268 8.380 1.00 30.04 AAAA ATOM 1211 N LEU A 168 11.243 −2.238 10.359 1.00 31.72 AAAA ATOM 1212 CA LEU A 168 12.159 −1.277 10.959 1.00 32.61 AAAA ATOM 1213 CB LEU A 168 11.714 −0.942 12.387 1.00 33.77 AAAA ATOM 1214 CG LEU A 168 10.490 −0.040 12.562 1.00 34.46 AAAA ATOM 1215 CD1 LEU A 168 10.141 0.076 14.041 1.00 35.50 AAAA ATOM 1216 CD2 LEU A 168 10.790 1.338 11.974 1.00 34.18 AAAA ATOM 1217 C LEU A 168 13.594 −1.790 10.986 1.00 32.72 AAAA ATOM 1218 O LEU A 168 14.538 −1.002 10.923 1.00 32.67 AAAA ATOM 1219 N ALA A 169 13.752 −3.109 11.076 1.00 33.35 AAAA ATOM 1220 CA ALA A 169 15.077 −3.725 11.138 1.00 34.36 AAAA ATOM 1221 CB ALA A 169 14.992 −5.054 11.883 1.00 33.96 AAAA ATOM 1222 C ALA A 169 15.746 −3.939 9.777 1.00 35.45 AAAA ATOM 1223 O ALA A 169 16.905 −4.362 9.713 1.00 36.53 AAAA ATOM 1224 N LEU A 170 15.030 −3.651 8.695 1.00 34.52 AAAA ATOM 1225 CA LEU A 170 15.590 −3.833 7.358 1.00 34.60 AAAA ATOM 1226 CB LEU A 170 14.577 −3.423 6.281 1.00 34.25 AAAA ATOM 1227 CG LEU A 170 13.363 −4.333 6.071 1.00 33.98 AAAA ATOM 1228 CD1 LEU A 170 12.393 −3.675 5.101 1.00 34.11 AAAA ATOM 1229 CD2 LEU A 170 13.820 −5.688 5.543 1.00 33.52 AAAA ATOM 1230 C LEU A 170 16.880 −3.042 7.163 1.00 34.41 AAAA ATOM 1231 O LEU A 170 17.001 −1.902 7.616 1.00 33.45 AAAA ATOM 1232 N PRO A 171 17.867 −3.648 6.486 1.00 34.33 AAAA ATOM 1233 CD PRO A 171 17.877 −5.028 5.971 1.00 34.76 AAAA ATOM 1234 CA PRO A 171 19.152 −2.988 6.233 1.00 35.17 AAAA ATOM 1235 CB PRO A 171 19.897 −4.005 5.366 1.00 34.52 AAAA ATOM 1236 CG PRO A 171 19.361 −5.308 5.844 1.00 34.60 AAAA ATOM 1237 C PRO A 171 18.938 −1.665 5.503 1.00 35.39 AAAA ATOM 1238 O PRO A 171 17.933 −1.485 4.820 1.00 34.32 AAAA ATOM 1239 N LEU A 172 19.884 −0.746 5.654 1.00 36.05 AAAA ATOM 1240 CA LEU A 172 19.801 0.555 4.998 1.00 37.43 AAAA ATOM 1241 CB LEU A 172 20.946 1.458 5.468 1.00 37.48 AAAA ATOM 1242 CG LEU A 172 20.934 1.934 6.925 1.00 38.42 AAAA ATOM 1243 CD1 LEU A 172 19.751 2.863 7.158 1.00 37.89 AAAA ATOM 1244 CD2 LEU A 172 20.876 0.735 7.859 1.00 38.70 AAAA ATOM 1245 C LEU A 172 19.865 0.400 3.479 1.00 38.03 AAAA ATOM 1246 O LEU A 172 20.392 −0.591 2.969 1.00 38.19 AAAA ATOM 1247 N PRO A 173 19.329 1.383 2.737 1.00 38.41 AAAA ATOM 1248 CD PRO A 173 18.647 2.586 3.248 1.00 38.12 AAAA ATOM 1249 CA PRO A 173 19.319 1.367 1.271 1.00 39.54 AAAA ATOM 1250 CB PRO A 173 18.853 2.778 0.923 1.00 38.97 AAAA ATOM 1251 CG PRO A 173 17.898 3.076 2.029 1.00 38.41 AAAA ATOM 1252 C PRO A 173 20.672 1.027 0.639 1.00 41.06 AAAA ATOM 1253 O PRO A 173 20.751 0.205 −0.276 1.00 41.26 AAAA ATOM 1254 N GLN A 174 21.734 1.659 1.127 1.00 42.31 AAAA ATOM 1255 CA GLN A 174 23.063 1.401 0.591 1.00 43.56 AAAA ATOM 1256 CB GLN A 174 24.118 2.219 1.343 1.00 45.08 AAAA ATOM 1257 CG GLN A 174 24.197 3.672 0.906 1.00 47.91 AAAA ATOM 1258 CD GLN A 174 25.366 4.413 1.534 1.00 50.04 AAAA ATOM 1259 OE1 GLN A 174 25.665 5.552 1.164 1.00 50.92 AAAA ATOM 1260 NE2 GLN A 174 26.033 3.771 2.491 1.00 50.23 AAAA ATOM 1261 C GLN A 174 23.415 −0.076 0.667 1.00 43.25 AAAA ATOM 1262 O GLN A 174 23.955 −0.641 −0.280 1.00 42.73 AAAA ATOM 1263 N GLN A 175 23.098 −0.702 1.794 1.00 43.02 AAAA ATOM 1264 CA GLN A 175 23.398 −2.115 1.981 1.00 43.41 AAAA ATOM 1265 CB GLN A 175 23.206 −2.505 3.449 1.00 44.88 AAAA ATOM 1266 CG GLN A 175 23.844 −1.544 4.444 1.00 47.91 AAAA ATOM 1267 CD GLN A 175 25.331 −1.344 4.211 1.00 49.82 AAAA ATOM 1268 OE1 GLN A 175 25.747 −0.765 3.203 1.00 50.30 AAAA ATOM 1269 NE2 GLN A 175 26.145 −1.826 5.148 1.00 51.04 AAAA ATOM 1270 C GLN A 175 22.521 −2.997 1.097 1.00 42.34 AAAA ATOM 1271 O GLN A 175 22.996 −3.961 0.500 1.00 41.64 AAAA ATOM 1272 N ARG A 176 21.238 −2.659 1.016 1.00 41.73 AAAA ATOM 1273 CA ARG A 176 20.285 −3.422 0.216 1.00 41.37 AAAA ATOM 1274 CB ARG A 176 18.854 −2.912 0.469 1.00 42.69 AAAA ATOM 1275 CG ARG A 176 17.767 −3.726 −0.232 1.00 44.32 AAAA ATOM 1276 CD ARG A 176 16.338 −3.227 0.066 1.00 46.28 AAAA ATOM 1277 NE ARG A 176 15.922 −2.116 −0.793 1.00 46.82 AAAA ATOM 1278 CZ ARG A 176 16.043 −0.829 −0.479 1.00 47.07 AAAA ATOM 1279 NH1 ARG A 176 16.567 −0.471 0.686 1.00 47.74 AAAA ATOM 1280 NH2 ARG A 176 15.645 0.102 −1.337 1.00 46.75 AAAA ATOM 1281 C ARG A 176 20.574 −3.358 −1.279 1.00 40.60 AAAA ATOM 1282 O ARG A 176 20.485 −4.366 −1.981 1.00 39.33 AAAA ATOM 1283 N LEU A 177 20.928 −2.171 −1.757 1.00 40.82 AAAA ATOM 1284 CA LEU A 177 21.182 −1.957 −3.177 1.00 41.69 AAAA ATOM 1285 CB LEU A 177 20.635 −0.587 −3.580 1.00 41.42 AAAA ATOM 1286 CG LEU A 177 19.152 −0.376 −3.262 1.00 41.85 AAAA ATOM 1287 CD1 LEU A 177 18.756 1.059 −3.578 1.00 41.44 AAAA ATOM 1288 CD2 LEU A 177 18.311 −1.358 −4.066 1.00 41.27 AAAA ATOM 1289 C LEU A 177 22.632 −2.080 −3.636 1.00 42.12 AAAA ATOM 1290 O LEU A 177 22.923 −1.918 −4.822 1.00 42.57 AAAA ATOM 1291 N ALA A 178 23.536 −2.374 −2.709 1.00 42.36 AAAA ATOM 1292 CA ALA A 178 24.951 −2.505 −3.047 1.00 41.77 AAAA ATOM 1293 CB ALA A 178 25.774 −2.711 −1.778 1.00 42.52 AAAA ATOM 1294 C ALA A 178 25.204 −3.649 −4.024 1.00 41.23 AAAA ATOM 1295 O ALA A 178 24.981 −4.818 −3.701 1.00 41.31 AAAA ATOM 1296 N GLY A 179 25.668 −3.299 −5.221 1.00 40.21 AAAA ATOM 1297 CA GLY A 179 25.960 −4.298 −6.232 1.00 37.93 AAAA ATOM 1298 C GLY A 179 24.747 −4.873 −6.938 1.00 36.85 AAAA ATOM 1299 O GLY A 179 24.873 −5.797 −7.744 1.00 36.55 AAAA ATOM 1300 N ARG A 180 23.566 −4.333 −6.654 1.00 35.52 AAAA ATOM 1301 CA ARG A 180 22.362 −4.844 −7.289 1.00 34.04 AAAA ATOM 1302 CB ARG A 180 21.114 −4.428 −6.504 1.00 31.99 AAAA ATOM 1303 CG ARG A 180 19.840 −5.038 −7.055 1.00 29.72 AAAA ATOM 1304 CD ARG A 180 18.608 −4.609 −6.268 1.00 27.51 AAAA ATOM 1305 NE ARG A 180 18.531 −5.233 −4.948 1.00 25.67 AAAA ATOM 1306 CZ ARG A 180 17.475 −5.139 −4.144 1.00 26.02 AAAA ATOM 1307 NH1 ARG A 180 16.414 −4.441 −4.533 1.00 24.19 AAAA ATOM 1308 NH2 ARG A 180 17.472 −5.749 −2.961 1.00 23.88 AAAA ATOM 1309 C ARG A 180 22.251 −4.353 −8.726 1.00 34.92 AAAA ATOM 1310 O ARG A 180 22.348 −3.157 −8.995 1.00 35.69 AAAA ATOM 1311 N GLU A 181 22.055 −5.290 −9.646 1.00 34.98 AAAA ATOM 1312 CA GLU A 181 21.917 −4.969 −11.059 1.00 35.58 AAAA ATOM 1313 CB GLU A 181 23.188 −5.354 −11.822 1.00 37.16 AAAA ATOM 1314 CG GLU A 181 24.411 −4.540 −11.436 1.00 40.11 AAAA ATOM 1315 CD GLU A 181 25.666 −4.983 −12.169 1.00 42.11 AAAA ATOM 1316 OE1 GLU A 181 26.698 −4.284 −12.056 1.00 42.94 AAAA ATOM 1317 OE2 GLU A 181 25.623 −6.033 −12.848 1.00 43.38 AAAA ATOM 1318 C GLU A 181 20.736 −5.745 −11.615 1.00 34.83 AAAA ATOM 1319 O GLU A 181 20.148 −6.577 −10.919 1.00 35.81 AAAA ATOM 1320 N GLY A 182 20.387 −5.469 − 12.866 1.00 33.11 AAAA ATOM 1321 CA GLY A 182 19.279 −6.166 −13.489 1.00 31.63 AAAA ATOM 1322 C GLY A 182 17.989 −5.368 −13.523 1.00 30.40 AAAA ATOM 1323 O GLY A 182 17.959 −4.210 −13.106 1.00 28.65 AAAA ATOM 1324 N PRO A 183 16.898 −5.974 −14.015 1.00 29.29 AAAA ATOM 1325 CD PRO A 183 16.829 −7.363 −14.498 1.00 30.43 AAAA ATOM 1326 CA PRO A 183 15.589 −5.327 −14.109 1.00 29.46 AAAA ATOM 1327 CB PRO A 183 14.675 −6.463 −14.560 1.00 29.59 AAAA ATOM 1328 CG PRO A 183 15.597 −7.333 −15.362 1.00 30.17 AAAA ATOM 1329 C PRO A 183 15.159 −4.734 −12.771 1.00 29.01 AAAA ATOM 1330 O PRO A 183 15.455 −5.289 −11.708 1.00 27.87 AAAA ATOM 1331 N VAL A 184 14.483 −3.591 −12.826 1.00 27.36 AAAA ATOM 1332 CA VAL A 184 14.014 −2.942 − 11.613 1.00 25.28 AAAA ATOM 1333 CB VAL A 184 13.506 −1.512 −11.912 1.00 26.16 AAAA ATOM 1334 CG1 VAL A 184 12.865 −0.901 −10.673 1.00 25.72 AAAA ATOM 1335 CG2 VAL A 184 14.670 −0.648 −12.374 1.00 26.35 AAAA ATOM 1336 C VAL A 184 12.896 −3.799 −11.032 1.00 23.68 AAAA ATOM 1337 O VAL A 184 11.971 −4.195 −11.735 1.00 21.69 AAAA ATOM 1338 N ARG A 185 13.003 −4.102 −9.744 1.00 23.12 AAAA ATOM 1339 CA ARG A 185 12.015 −4.931 −9.065 1.00 22.35 AAAA ATOM 1340 CB ARG A 185 12.687 −5.649 −7.897 1.00 23.23 AAAA ATOM 1341 CG ARG A 185 13.910 −6.440 −8.323 1.00 25.75 AAAA ATOM 1342 CD ARG A 185 14.729 −6.847 −7.120 1.00 27.07 AAAA ATOM 1343 NE ARG A 185 15.976 −7.502 −7.495 1.00 28.67 AAAA ATOM 1344 CZ ARG A 185 16.784 −8.093 −6.623 1.00 29.19 AAAA ATOM 1345 NH1 ARG A 185 16.462 −8.100 −5.339 1.00 26.72 AAAA ATOM 1346 NH2 ARG A 185 17.903 −8.679 −7.032 1.00 31.00 AAAA ATOM 1347 C ARG A 185 10.860 −4.066 −8.574 1.00 21.55 AAAA ATOM 1348 O ARG A 185 11.033 −3.228 −7.693 1.00 21.13 AAAA ATOM 1349 N VAL A 186 9.687 −4.263 −9.166 1.00 21.59 AAAA ATOM 1350 CA VAL A 186 8.515 −3.480 −8.805 1.00 21.51 AAAA ATOM 1351 CB VAL A 186 7.745 −3.005 −10.064 1.00 21.61 AAAA ATOM 1352 CG1 VAL A 186 6.574 −2.124 −9.656 1.00 21.27 AAAA ATOM 1353 CG2 VAL A 186 8.689 −2.252 −11.001 1.00 22.25 AAAA ATOM 1354 C VAL A 186 7.563 −4.294 −7.942 1.00 20.09 AAAA ATOM 1355 O VAL A 186 7.064 −5.330 −8.361 1.00 20.16 AAAA ATOM 1356 N LEU A 187 7.325 −3.807 −6.735 1.00 20.75 AAAA ATOM 1357 CA LEU A 187 6.421 −4.462 −5.801 1.00 21.10 AAAA ATOM 1358 CB LEU A 187 6.979 −4.363 −4.379 1.00 22.77 AAAA ATOM 1359 CG LEU A 187 6.492 −5.359 −3.316 1.00 24.90 AAAA ATOM 1360 CD1 LEU A 187 6.763 −4.768 −1.932 1.00 23.74 AAAA ATOM 1361 CD2 LEU A 187 5.027 −5.651 −3.487 1.00 27.67 AAAA ATOM 1362 C LEU A 187 5.104 −3.691 −5.871 1.00 21.37 AAAA ATOM 1363 O LEU A 187 5.078 −2.491 −5.585 1.00 21.09 AAAA ATOM 1364 N VAL A 188 4.034 −4.377 −6.262 1.00 21.43 AAAA ATOM 1365 CA VAL A 188 2.706 −3.774 −6.355 1.00 22.58 AAAA ATOM 1366 CB VAL A 188 1.988 −4.190 −7.657 1.00 22.95 AAAA ATOM 1367 CG1 VAL A 188 0.643 −3.488 −7.765 1.00 22.98 AAAA ATOM 1368 CG2 VAL A 188 2.853 −3.842 −8.855 1.00 23.03 AAAA ATOM 1369 C VAL A 188 1.891 −4.267 −5.161 1.00 22.98 AAAA ATOM 1370 O VAL A 188 1.603 −5.456 −5.051 1.00 22.38 AAAA ATOM 1371 N VAL A 189 1.534 −3.349 −4.267 1.00 23.91 AAAA ATOM 1372 CA VAL A 189 0.779 −3.706 −3.070 1.00 25.11 AAAA ATOM 1373 CB VAL A 189 1.523 −3.237 −1.800 1.00 25.30 AAAA ATOM 1374 CG1 VAL A 189 0.740 −3.635 −0.549 1.00 23.23 AAAA ATOM 1375 CG2 VAL A 189 2.915 −3.828 −1.773 1.00 22.20 AAAA ATOM 1376 C VAL A 189 −0.619 −3.096 −3.080 1.00 26.20 AAAA ATOM 1377 O VAL A 189 −0.770 −1.879 −3.186 1.00 26.94 AAAA ATOM 1378 N GLY A 190 −1.629 −3.955 −2.975 1.00 27.50 AAAA ATOM 1379 CA GLY A 190 −3.007 −3.505 −2.966 1.00 30.27 AAAA ATOM 1380 C GLY A 190 −3.720 −3.736 −1.641 1.00 32.15 AAAA ATOM 1381 O GLY A 190 −4.896 −3.403 −1.499 1.00 32.00 AAAA ATOM 1382 N GLY A 191 −3.016 −4.299 −0.664 1.00 32.97 AAAA ATOM 1383 CA GLY A 191 −3.640 −4.550 0.624 1.00 34.29 AAAA ATOM 1384 C GLY A 191 −4.507 −5.794 0.607 1.00 34.92 AAAA ATOM 1385 O GLY A 191 −4.741 −6.388 −0.444 1.00 34.34 AAAA ATOM 1386 N SER A 192 −4.996 −6.183 1.778 1.00 36.47 AAAA ATOM 1387 CA SER A 192 −5.827 −7.377 1.910 1.00 38.39 AAAA ATOM 1388 CB SER A 192 −6.389 −7.460 3.335 1.00 39.07 AAAA ATOM 1389 OG SER A 192 −7.124 −6.291 3.658 1.00 41.25 AAAA ATOM 1390 C SER A 192 −6.974 −7.472 0.903 1.00 38.69 AAAA ATOM 1391 O SER A 192 −7.293 −8.557 0.410 1.00 38.58 AAAA ATOM 1392 N GLN A 193 −7.599 −6.344 0.595 1.00 38.60 AAAA ATOM 1393 CA GLN A 193 −8.715 −6.367 −0.339 1.00 39.91 AAAA ATOM 1394 CB GLN A 193 −9.787 −5.367 0.110 1.00 41.97 AAAA ATOM 1395 CG GLN A 193 −10.354 −5.679 1.497 1.00 43.94 AAAA ATOM 1396 CD GLN A 193 −10.790 −7.135 1.640 1.00 45.71 AAAA ATOM 1397 OE1 GLN A 193 −11.677 −7.607 0.922 1.00 46.93 AAAA ATOM 1398 NE2 GLN A 193 −10.162 −7.853 2.567 1.00 45.80 AAAA ATOM 1399 C GLN A 193 −8.298 −6.098 −1.781 1.00 39.31 AAAA ATOM 1400 O GLN A 193 −9.076 −6.320 −2.708 1.00 39.52 AAAA ATOM 1401 N GLY A 194 −7.064 −5.642 −1.961 1.00 38.40 AAAA ATOM 1402 CA GLY A 194 −6.560 −5.358 −3.291 1.00 38.11 AAAA ATOM 1403 C GLY A 194 −6.961 −3.987 −3.797 1.00 37.62 AAAA ATOM 1404 O GLY A 194 −7.904 −3.382 −3.291 1.00 37.80 AAAA ATOM 1405 N ALA A 195 −6.228 −3.489 −4.787 1.00 36.62 AAAA ATOM 1406 CA ALA A 195 −6.513 −2.191 −5.387 1.00 36.35 AAAA ATOM 1407 CB ALA A 195 −5.290 −1.291 −5.305 1.00 35.75 AAAA ATOM 1408 C ALA A 195 −6.898 −2.437 −6.842 1.00 36.61 AAAA ATOM 1409 O ALA A 195 −6.038 −2.519 −7.717 1.00 35.93 AAAA ATOM 1410 N ARG A 196 −8.198 −2.566 −7.080 1.00 36.94 AAAA ATOM 1411 CA ARG A 196 −8.741 −2.828 −8.412 1.00 38.03 AAAA ATOM 1412 CB ARG A 196 −10.229 −2.466 −8.450 1.00 40.33 AAAA ATOM 1413 CG ARG A 196 −10.526 −0.968 −8.375 1.00 44.08 AAAA ATOM 1414 CD ARG A 196 −9.935 −0.306 −7.129 1.00 46.46 AAAA ATOM 1415 NE ARG A 196 −10.381 −0.949 −5.894 1.00 48.33 AAAA ATOM 1416 CZ ARG A 196 −10.199 −0.439 −4.682 1.00 48.85 AAAA ATOM 1417 NH1 ARG A 196 −9.581 0.725 −4.538 1.00 49.51 AAAA ATOM 1418 NH2 ARG A 196 −10.636 −1.093 −3.615 1.00 49.95 AAAA ATOM 1419 C ARG A 196 −8.023 −2.120 −9.558 1.00 37.11 AAAA ATOM 1420 O ARG A 196 −7.729 −2.736 −10.583 1.00 36.96 AAAA ATOM 1421 N ILE A 197 −7.739 −0.834 −9.392 1.00 35.89 AAAA ATOM 1422 CA ILE A 197 −7.071 −0.091 −10.448 1.00 35.67 AAAA ATOM 1423 CB ILE A 197 −7.049 1.427 −10.161 1.00 36.70 AAAA ATOM 1424 CG2 ILE A 197 −6.221 1.726 −8.918 1.00 36.91 AAAA ATOM 1425 CG1 ILE A 197 −6.485 2.162 −11.381 1.00 36.95 AAAA ATOM 1426 CD1 ILE A 197 −6.529 3.661 −11.272 1.00 38.71 AAAA ATOM 1427 C ILE A 197 −5.644 −0.580 −10.694 1.00 34.73 AAAA ATOM 1428 O ILE A 197 −5.178 −0.575 −11.833 1.00 33.53 AAAA ATOM 1429 N LEU A 198 −4.948 −0.992 −9.638 1.00 32.35 AAAA ATOM 1430 CA LEU A 198 −3.588 −1.494 −9.813 1.00 31.48 AAAA ATOM 1431 CB LEU A 198 −2.862 −1.633 −8.467 1.00 31.03 AAAA ATOM 1432 CG LEU A 198 −2.548 −0.342 −7.704 1.00 32.00 AAAA ATOM 1433 CD1 LEU A 198 −1.773 −0.688 −6.442 1.00 30.82 AAAA ATOM 1434 CD2 LEU A 198 −1.734 0.607 −8.566 1.00 30.86 AAAA ATOM 1435 C LEU A 198 −3.668 −2.850 −10.501 1.00 29.72 AAAA ATOM 1436 O LEU A 198 −2.837 −3.173 −11.344 1.00 29.46 AAAA ATOM 1437 N ASN A 199 −4.678 −3.639 −10.150 1.00 28.63 AAAA ATOM 1438 CA ASN A 199 −4.848 −4.952 −10.758 1.00 28.66 AAAA ATOM 1439 CB ASN A 199 −5.975 −5.724 −10.066 1.00 27.71 AAAA ATOM 1440 CG ASN A 199 −5.641 −6.069 −8.632 1.00 26.12 AAAA ATOM 1441 OD1 ASN A 199 −4.501 −5.904 −8.200 1.00 24.15 AAAA ATOM 1442 ND2 ASN A 199 −6.631 −6.553 −7.834 1.00 24.90 AAAA ATOM 1443 C ASN A 199 −5.144 −4.841 −12.248 1.00 29.87 AAAA ATOM 1444 O ASN A 199 −4.834 −5.747 −13.024 1.00 30.26 AAAA ATOM 1445 N GLN A 200 −5.746 −3.725 −12.644 1.00 31.15 AAAA ATOM 1446 CA GLN A 200 −6.085 −3.498 −14.044 1.00 33.06 AAAA ATOM 1447 CB GLN A 200 −7.396 −2.706 −14.145 1.00 34.24 AAAA ATOM 1448 CG GLN A 200 −8.590 −3.368 −13.471 1.00 38.64 AAAA ATOM 1449 CD GLN A 200 −8.923 −4.734 −14.050 1.00 41.05 AAAA ATOM 1450 OE1 GLN A 200 −9.131 −4.879 −15.256 1.00 43.10 AAAA ATOM 1451 NE2 GLN A 200 −8.983 −5.745 −13.185 1.00 43.12 AAAA ATOM 1452 C GLN A 200 −4.989 −2.753 −14.812 1.00 32.52 AAAA ATOM 1453 O GLN A 200 −4.809 −2.970 −16.008 1.00 34.23 AAAA ATOM 1454 N THR A 201 −4.247 −1.895 −14.120 1.00 31.87 AAAA ATOM 1455 CA THR A 201 −3.207 −1.092 −14.756 1.00 31.72 AAAA ATOM 1456 CB THR A 201 −3.046 0.245 −13.999 1.00 32.41 AAAA ATOM 1457 OG1 THR A 201 −4.307 0.931 −13.976 1.00 32.19 AAAA ATOM 1458 CG2 THR A 201 −2.003 1.131 −14.668 1.00 32.29 AAAA ATOM 1459 C THR A 201 −1.817 −1.728 −14.925 1.00 32.02 AAAA ATOM 1460 O THR A 201 −1.206 −1.626 −15.991 1.00 31.47 AAAA ATOM 1461 N MET A 202 −1.320 −2.394 −13.892 1.00 30.61 AAAA ATOM 1462 CA MET A 202 0.019 −2.975 −13.963 1.00 30.10 AAAA ATOM 1463 CB MET A 202 0.430 −3.507 −12.592 1.00 29.71 AAAA ATOM 1464 CG MET A 202 0.564 −2.406 −11.548 1.00 28.99 AAAA ATOM 1465 SD MET A 202 1.518 −0.961 −12.098 1.00 31.46 AAAA ATOM 1466 CE MET A 202 3.184 −1.633 −12.184 1.00 29.20 AAAA ATOM 1467 C MET A 202 0.286 −4.022 −15.042 1.00 29.48 AAAA ATOM 1468 O MET A 202 1.389 −4.088 −15.568 1.00 29.15 AAAA ATOM 1469 N PRO A 203 −0.703 −4.863 −15.379 1.00 30.34 AAAA ATOM 1470 CD PRO A 203 −1.957 −5.186 −14.677 1.00 30.05 AAAA ATOM 1471 CA PRO A 203 −0.415 −5.849 −16.426 1.00 31.11 AAAA ATOM 1472 CB PRO A 203 −1.703 −6.654 −16.500 1.00 31.89 AAAA ATOM 1473 CG PRO A 203 −2.188 −6.623 −15.072 1.00 31.09 AAAA ATOM 1474 C PRO A 203 −0.103 −5.139 −17.746 1.00 33.02 AAAA ATOM 1475 O PRO A 203 0.800 −5.530 −18.490 1.00 33.16 AAAA ATOM 1476 N GLN A 204 −0.855 −4.081 −18.020 1.00 33.88 AAAA ATOM 1477 CA GLN A 204 −0.666 −3.314 −19.242 1.00 34.99 AAAA ATOM 1478 CB GLN A 204 −1.836 −2.347 −19.431 1.00 37.12 AAAA ATOM 1479 CG GLN A 204 −3.177 −3.067 −19.538 1.00 40.86 AAAA ATOM 1480 CD GLN A 204 −4.354 −2.121 −19.700 1.00 43.77 AAAA ATOM 1481 OE1 GLN A 204 −4.406 −1.330 −20.647 1.00 45.55 AAAA ATOM 1482 NE2 GLN A 204 −5.310 −2.198 −18.776 1.00 44.11 AAAA ATOM 1483 C GLN A 204 0.659 −2.573 − 19.190 1.00 33.42 AAAA ATOM 1484 O GLN A 204 1.331 −2.431 − 20.206 1.00 34.40 AAAA ATOM 1485 N VAL A 205 1.045 −2.114 − 18.002 1.00 32.44 AAAA ATOM 1486 CA VAL A 205 2.313 −1.417 − 17.836 1.00 30.42 AAAA ATOM 1487 CB VAL A 205 2.466 −0.834 − 16.408 1.00 31.72 AAAA ATOM 1488 CG1 VAL A 205 3.907 −0.406 − 16.169 1.00 28.58 AAAA ATOM 1489 CG2 VAL A 205 1.544 0.356 − 16.231 1.00 29.91 AAAA ATOM 1490 C VAL A 205 3.446 −2.407 − 18.086 1.00 30.65 AAAA ATOM 1491 O VAL A 205 4.473 −2.062 − 18.686 1.00 29.65 AAAA ATOM 1492 N ALA A 206 3.255 −3.638 − 17.616 1.00 29.08 AAAA ATOM 1493 CA ALA A 206 4.253 −4.688 − 17.796 1.00 30.43 AAAA ATOM 1494 CB ALA A 206 3.763 −6.002 − 17.169 1.00 27.77 AAAA ATOM 1495 C ALA A 206 4.519 −4.886 − 19.288 1.00 30.65 AAAA ATOM 1496 O ALA A 206 5.668 −5.040 − 19.709 1.00 30.70 AAAA ATOM 1497 N ALA A 207 3.450 −4.879 − 20.080 1.00 31.56 AAAA ATOM 1498 CA ALA A 207 3.565 −5.053 −21.527 1.00 32.70 AAAA ATOM 1499 CB ALA A 207 2.188 −4.997 −22.167 1.00 32.49 AAAA ATOM 1500 C ALA A 207 4.470 −3.990 −22.145 1.00 32.72 AAAA ATOM 1501 O ALA A 207 5.295 −4.284 −23.007 1.00 33.64 AAAA ATOM 1502 N LYS A 208 4.321 −2.754 −21.692 1.00 33.07 AAAA ATOM 1503 CA LYS A 208 5.112 −1.651 −22.216 1.00 33.20 AAAA ATOM 1504 CB LYS A 208 4.477 −0.313 −21.814 1.00 35.14 AAAA ATOM 1505 CG LYS A 208 3.199 0.044 −22.578 1.00 38.07 AAAA ATOM 1506 CD LYS A 208 2.166 −1.062 −22.482 1.00 40.27 AAAA ATOM 1507 CE LYS A 208 0.892 −0.731 −23.233 1.00 41.02 AAAA ATOM 1508 NZ LYS A 208 −0.076 −1.857 −23.126 1.00 42.41 AAAA ATOM 1509 C LYS A 208 6.571 −1.668 −21.779 1.00 32.58 AAAA ATOM 1510 O LYS A 208 7.456 −1.274 −22.544 1.00 31.82 AAAA ATOM 1511 N LEU A 209 6.829 −2.121 − 20.556 1.00 30.72 AAAA ATOM 1512 CA LEU A 209 8.193 −2.143 − 20.042 1.00 30.48 AAAA ATOM 1513 CB LEU A 209 8.191 −1.848 − 18.535 1.00 29.34 AAAA ATOM 1514 CG LEU A 209 7.596 −0.498 − 18.107 1.00 31.02 AAAA ATOM 1515 CD1 LEU A 209 7.779 −0.318 − 16.605 1.00 29.42 AAAA ATOM 1516 CD2 LEU A 209 8.273 0.641 − 18.859 1.00 31.39 AAAA ATOM 1517 C LEU A 209 8.970 −3.432 − 20.315 1.00 29.73 AAAA ATOM 1518 O LEU A 209 10.191 −3.455 − 20.174 1.00 31.33 AAAA ATOM 1519 N GLY A 210 8.269 −4.494 − 20.698 1.00 29.76 AAAA ATOM 1520 CA GLY A 210 8.924 −5.762 − 20.986 1.00 29.99 AAAA ATOM 1521 C GLY A 210 10.007 −6.188 − 20.003 1.00 30.99 AAAA ATOM 1522 O GLY A 210 9.788 −6.183 − 18.789 1.00 30.80 AAAA ATOM 1523 N ASP A 211 11.181 −6.536 − 20.535 1.00 30.05 AAAA ATOM 1524 CA ASP A 211 12.332 −6.999 − 19.749 1.00 29.42 AAAA ATOM 1525 CB ASP A 211 13.466 −7.479 − 20.676 1.00 30.83 AAAA ATOM 1526 CG ASP A 211 13.119 −8.735 −21.449 1.00 32.09 AAAA ATOM 1527 OD1 ASP A 211 13.977 −9.193 −22.235 1.00 34.13 AAAA ATOM 1528 OD2 ASP A 211 12.005 −9.269 −21.283 1.00 32.72 AAAA ATOM 1529 C ASP A 211 12.960 −6.011 − 18.776 1.00 29.03 AAAA ATOM 1530 O ASP A 211 13.781 −6.417 − 17.945 1.00 27.69 AAAA ATOM 1531 N SER A 212 12.613 −4.730 − 18.876 1.00 28.54 AAAA ATOM 1532 CA SER A 212 13.204 −3.719 − 18.002 1.00 27.61 AAAA ATOM 1533 CB SER A 212 12.927 −2.308 − 18.538 1.00 28.62 AAAA ATOM 1534 OG SER A 212 11.546 −1.990 − 18.498 1.00 30.84 AAAA ATOM 1535 C SER A 212 12.759 −3.805 − 16.542 1.00 26.31 AAAA ATOM 1536 O SER A 212 13.395 −3.219 − 15.666 1.00 25.39 AAAA ATOM 1537 N VAL A 213 11.675 −4.528 − 16.284 1.00 25.65 AAAA ATOM 1538 CA VAL A 213 11.187 −4.671 −14.914 1.00 24.52 AAAA ATOM 1539 CB VAL A 213 9.967 −3.747 −14.621 1.00 25.58 AAAA ATOM 1540 CG1 VAL A 213 10.296 −2.298 −14.953 1.00 26.31 AAAA ATOM 1541 CG2 VAL A 213 8.758 −4.225 −15.394 1.00 25.15 AAAA ATOM 1542 C VAL A 213 10.751 −6.095 −14.607 1.00 23.77 AAAA ATOM 1543 O VAL A 213 10.427 −6.874 −15.506 1.00 23.79 AAAA ATOM 1544 N THR A 214 10.770 −6.432 −13.323 1.00 23.49 AAAA ATOM 1545 CA THR A 214 10.326 −7.735 −12.861 1.00 21.50 AAAA ATOM 1546 CB THR A 214 11.499 −8.600 −12.325 1.00 21.99 AAAA ATOM 1547 OG1 THR A 214 10.987 −9.870 −11.909 1.00 23.56 AAAA ATOM 1548 CG2 THR A 214 12.220 −7.921 −11.174 1.00 20.60 AAAA ATOM 1549 C THR A 214 9.342 −7.362 −11.760 1.00 21.46 AAAA ATOM 1550 O THR A 214 9.657 −6.567 −10.880 1.00 21.12 AAAA ATOM 1551 N ILE A 215 8.150 −7.938 −11.827 1.00 21.73 AAAA ATOM 1552 CA ILE A 215 7.083 −7.601 −10.894 1.00 22.01 AAAA ATOM 1553 CB ILE A 215 5.831 −7.139 −11.688 1.00 22.41 AAAA ATOM 1554 CG2 ILE A 215 4.707 −6.738 −10.734 1.00 22.94 AAAA ATOM 1555 CG1 ILE A 215 6.198 −5.964 −12.599 1.00 22.71 AAAA ATOM 1556 CD1 ILE A 215 5.078 −5.560 −13.545 1.00 21.71 AAAA ATOM 1557 C ILE A 215 6.617 −8.685 −9.929 1.00 21.67 AAAA ATOM 1558 O ILE A 215 6.600 −9.868 −10.257 1.00 20.14 AAAA ATOM 1559 N TRP A 216 6.248 −8.247 −8.728 1.00 21.03 AAAA ATOM 1560 CA TRP A 216 5.677 −9.121 −7.708 1.00 21.08 AAAA ATOM 1561 CB TRP A 216 6.541 −9.186 −6.455 1.00 21.14 AAAA ATOM 1562 CG TRP A 216 5.941 −10.063 −5.370 1.00 21.49 AAAA ATOM 1563 CD2 TRP A 216 6.624 −10.588 −4.226 1.00 21.97 AAAA ATOM 1564 CE2 TRP A 216 5.674 −11.309 −3.461 1.00 22.67 AAAA ATOM 1565 CE3 TRP A 216 7.947 −10.521 −3.773 1.00 22.25 AAAA ATOM 1566 CD1 TRP A 216 4.639 −10.478 −5.262 1.00 21.72 AAAA ATOM 1567 NE1 TRP A 216 4.472 −11.231 −4.112 1.00 22.34 AAAA ATOM 1568 CZ2 TRP A 216 6.011 −11.955 −2.265 1.00 24.81 AAAA ATOM 1569 CZ3 TRP A 216 8.283 −11.166 −2.582 1.00 23.37 AAAA ATOM 1570 CH2 TRP A 216 7.316 −11.872 −1.843 1.00 23.19 AAAA ATOM 1571 C TRP A 216 4.401 −8.352 −7.396 1.00 21.75 AAAA ATOM 1572 O TRP A 216 4.442 −7.330 −6.719 1.00 22.71 AAAA ATOM 1573 N HIS A 217 3.280 −8.844 −7.909 1.00 23.00 AAAA ATOM 1574 CA HIS A 217 1.987 −8.185 −7.751 1.00 24.05 AAAA ATOM 1575 CB HIS A 217 1.301 −8.167 −9.127 1.00 25.31 AAAA ATOM 1576 CG HIS A 217 0.075 −7.312 −9.201 1.00 27.29 AAAA ATOM 1577 CD2 HIS A 217 −1.008 −7.226 −8.391 1.00 27.56 AAAA ATOM 1578 ND1 HIS A 217 −0.146 −6.424 −10.233 1.00 28.22 AAAA ATOM 1579 CE1 HIS A 217 −1.311 −5.828 −10.057 1.00 28.76 AAAA ATOM 1580 NE2 HIS A 217 −1.856 −6.296 −8.947 1.00 27.39 AAAA ATOM 1581 C HIS A 217 1.095 −8.880 −6.714 1.00 22.49 AAAA ATOM 1582 O HIS A 217 0.785 − 10.059 −6.851 1.00 24.60 AAAA ATOM 1583 N GLN A 218 0.696 −8.144 −5.679 1.00 24.33 AAAA ATOM 1584 CA GLN A 218 −0.184 −8.676 −4.629 1.00 24.84 AAAA ATOM 1585 CB GLN A 218 0.271 −8.181 −3.250 1.00 25.16 AAAA ATOM 1586 CG GLN A 218 −0.572 −8.709 −2.084 1.00 26.40 AAAA ATOM 1587 CD GLN A 218 −1.629 −7.722 −1.608 1.00 27.63 AAAA ATOM 1588 OE1 GLN A 218 −2.762 −8.107 −1.297 1.00 29.31 AAAA ATOM 1589 NE2 GLN A 218 −1.260 −6.455 −1.525 1.00 24.88 AAAA ATOM 1590 C GLN A 218 −1.573 −8.134 −4.983 1.00 24.83 AAAA ATOM 1591 O GLN A 218 −1.859 −6.960 −4.767 1.00 24.21 AAAA ATOM 1592 N SER A 219 −2.413 −9.008 −5.531 1.00 25.76 AAAA ATOM 1593 CA SER A 219 −3.745 −8.658 −6.022 1.00 27.99 AAAA ATOM 1594 CB SER A 219 −4.189 −9.704 −7.035 1.00 28.46 AAAA ATOM 1595 OG SER A 219 −4.394 −10.949 −6.387 1.00 29.92 AAAA ATOM 1596 C SER A 219 −4.887 −8.470 −5.034 1.00 29.52 AAAA ATOM 1597 O SER A 219 −5.842 −7.745 −5.321 1.00 29.47 AAAA ATOM 1598 N GLY A 220 −4.806 −9.135 −3.890 1.00 30.25 AAAA ATOM 1599 CA GLY A 220 −5.874 −9.031 −2.919 1.00 31.33 AAAA ATOM 1600 C GLY A 220 −6.696 −10.302 −2.952 1.00 32.52 AAAA ATOM 1601 O GLY A 220 −6.554 −11.126 −3.862 1.00 31.13 AAAA ATOM 1602 N LYS A 221 −7.563 −10.452 −1.956 1.00 33.12 AAAA ATOM 1603 CA LYS A 221 −8.423 −11.619 −1.815 1.00 34.69 AAAA ATOM 1604 CB LYS A 221 −9.340 −11.421 −0.601 1.00 35.93 AAAA ATOM 1605 CG LYS A 221 −10.257 −12.593 −0.285 1.00 38.70 AAAA ATOM 1606 CD LYS A 221 −11.079 −12.292 0.966 1.00 40.53 AAAA ATOM 1607 CE LYS A 221 −11.955 −13.465 1.368 1.00 41.74 AAAA ATOM 1608 NZ LYS A 221 −12.724 −13.160 2.614 1.00 43.70 AAAA ATOM 1609 C LYS A 221 −9.269 −11.932 −3.046 1.00 34.22 AAAA ATOM 1610 O LYS A 221 −9.979 − 11.070 −3.561 1.00 34.62 AAAA ATOM 1611 N GLY A 222 −9.189 − 13.180 −3.500 1.00 34.61 AAAA ATOM 1612 CA GLY A 222 −9.956 − 13.622 −4.651 1.00 34.89 AAAA ATOM 1613 C GLY A 222 −9.598 − 13.027 −6.000 1.00 35.07 AAAA ATOM 1614 O GLY A 222 −10.325 − 13.231 −6.974 1.00 35.62 AAAA ATOM 1615 N SER A 223 −8.482 − 12.309 −6.083 1.00 35.16 AAAA ATOM 1616 CA SER A 223 −8.083 − 11.691 −7.349 1.00 35.04 AAAA ATOM 1617 CB SER A 223 −7.959 − 10.175 −7.173 1.00 35.18 AAAA ATOM 1618 OG SER A 223 −9.222 −9.593 −6.913 1.00 36.67 AAAA ATOM 1619 C SER A 223 −6.783 − 12.226 −7.949 1.00 34.73 AAAA ATOM 1620 O SER A 223 −6.343 − 11.758 −9.002 1.00 33.65 AAAA ATOM 1621 N GLN A 224 −6.176 − 13.202 −7.285 1.00 34.35 AAAA ATOM 1622 CA GLN A 224 −4.922 − 13.779 −7.753 1.00 34.39 AAAA ATOM 1623 CB GLN A 224 −4.493 − 14.910 −6.810 1.00 35.22 AAAA ATOM 1624 CG GLN A 224 −3.016 − 15.304 −6.895 1.00 34.71 AAAA ATOM 1625 CD GLN A 224 −2.656 −5.983 −8.199 1.00 35.46 AAAA ATOM 1626 OE1 GLN A 224 −3.386 − 16.844 −8.680 1.00 35.81 AAAA ATOM 1627 NE2 GLN A 224 −1.512 − 15.610 −8.772 1.00 36.28 AAAA ATOM 1628 C GLN A 224 −5.033 − 14.301 −9.188 1.00 35.00 AAAA ATOM 1629 O GLN A 224 −4.256 − 13.915 − 10.062 1.00 33.23 AAAA ATOM 1630 N GLN A 225 −6.018 − 15.160 −9.432 1.00 35.33 AAAA ATOM 1631 CA GLN A 225 −6.208 − 15.747 − 10.752 1.00 36.18 AAAA ATOM 1632 CB GLN A 225 −7.251 − 16.871 − 10.675 1.00 38.35 AAAA ATOM 1633 CG GLN A 225 −6.692 − 18.174 − 10.103 1.00 40.67 AAAA ATOM 1634 CD GLN A 225 −7.732 − 19.274 −9.983 1.00 43.02 AAAA ATOM 1635 OE1 GLN A 225 −8.418 − 19.609 −10.952 1.00 44.03 AAAA ATOM 1636 NE2 GLN A 225 −7.846 − 19.850 −8.789 1.00 43.72 AAAA ATOM 1637 C GLN A 225 −6.554 − 14.790 − 11.893 1.00 35.81 AAAA ATOM 1638 O GLN A 225 −6.113 − 15.001 − 13.023 1.00 35.91 AAAA ATOM 1639 N SER A 226 −7.325 − 13.741 − 11.619 1.00 34.00 AAAA ATOM 1640 CA SER A 226 −7.689 − 12.804 − 12.683 1.00 34.21 AAAA ATOM 1641 CB SER A 226 −8.865 − 11.920 − 12.251 1.00 34.12 AAAA ATOM 1642 OG SER A 226 −8.460 − 10.954 − 11.300 1.00 36.16 AAAA ATOM 1643 C SER A 226 −6.502 − 11.926 − 13.090 1.00 32.76 AAAA ATOM 1644 O SER A 226 −6.343 − 11.580 − 14.260 1.00 32.64 AAAA ATOM 1645 N VAL A 227 −5.669 − 11.566 − 12.121 1.00 31.82 AAAA ATOM 1646 CA VAL A 227 −4.498 − 10.737 − 12.400 1.00 30.69 AAAA ATOM 1647 CB VAL A 227 −3.942 − 10.117 − 11.102 1.00 29.27 AAAA ATOM 1648 CG1 VAL A 227 −2.619 −9.413 − 11.370 1.00 29.04 AAAA ATOM 1649 CG2 VAL A 227 −4.951 −9.117 − 10.546 1.00 29.09 AAAA ATOM 1650 C VAL A 227 −3.418 − 11.577 − 13.082 1.00 30.43 AAAA ATOM 1651 O VAL A 227 −2.716 − 11.103 − 13.973 1.00 29.50 AAAA ATOM 1652 N GLU A 228 −3.297 − 12.824 − 12.644 1.00 30.82 AAAA ATOM 1653 CA GLU A 228 −2.333 − 13.766 − 13.198 1.00 31.96 AAAA ATOM 1654 CB GLU A 228 −2.456 − 15.108 − 12.464 1.00 31.67 AAAA ATOM 1655 CG GLU A 228 −1.607 − 16.231 − 13.020 1.00 33.79 AAAA ATOM 1656 CD GLU A 228 −0.159 − 16.176 − 12.559 1.00 34.94 AAAA ATOM 1657 OE1 GLU A 228 0.631 − 17.041 − 12.998 1.00 36.44 AAAA ATOM 1658 OE2 GLU A 228 0.190 − 15.280 − 11.761 1.00 35.02 AAAA ATOM 1659 C GLU A 228 −2.658 − 13.944 − 14.685 1.00 32.05 AAAA ATOM 1660 O GLU A 228 −1.770 − 13.942 − 15.539 1.00 32.57 AAAA ATOM 1661 N GLN A 229 −3.945 − 14.082 − 14.981 1.00 31.94 AAAA ATOM 1662 CA GLN A 229 −4.405 − 14.255 − 16.351 1.00 32.98 AAAA ATOM 1663 CB GLN A 229 −5.896 − 14.616 − 16.359 1.00 35.59 AAAA ATOM 1664 CG GLN A 229 −6.375 − 15.211 − 17.674 1.00 39.28 AAAA ATOM 1665 CD GLN A 229 −7.825 − 15.665 − 17.623 1.00 41.31 AAAA ATOM 1666 OE1 GLN A 229 −8.317 − 16.307 − 18.553 1.00 43.67 AAAA ATOM 1667 NE2 GLN A 229 −8.516 − 15.332 −16.538 1.00 43.19 AAAA ATOM 1668 C GLN A 229 −4.171 − 12.982 −17.154 1.00 31.60 AAAA ATOM 1669 O GLN A 229 −3.878 − 13.037 −18.348 1.00 32.04 AAAA ATOM 1670 N ALA A 230 −4.296 − 11.836 − 16.490 1.00 30.96 AAAA ATOM 1671 CA ALA A 230 −4.092 − 10.542 − 17.131 1.00 30.04 AAAA ATOM 1672 CB ALA A 230 −4.453 −9.423 − 16.165 1.00 30.37 AAAA ATOM 1673 C ALA A 230 −2.649 − 10.379 − 17.598 1.00 29.65 AAAA ATOM 1674 O ALA A 230 −2.392 −9.869 − 18.689 1.00 29.50 AAAA ATOM 1675 N TYR A 231 −1.706 −10.802 − 16.762 1.00 27.99 AAAA ATOM 1676 CA TYR A 231 −0.295 − 10.707 − 17.111 1.00 27.27 AAAA ATOM 1677 CB TYR A 231 0.571 − 11.065 − 15.898 1.00 26.63 AAAA ATOM 1678 CG TYR A 231 0.829 −9.898 − 14.975 1.00 24.33 AAAA ATOM 1679 CD1 TYR A 231 1.687 −8.866 − 15.354 1.00 22.96 AAAA ATOM 1680 CE1 TYR A 231 1.926 −7.786 − 14.520 1.00 22.17 AAAA ATOM 1681 CD2 TYR A 231 0.210 −9.817 − 13.725 1.00 24.32 AAAA ATOM 1682 CE2 TYR A 231 0.442 −8.737 − 12.879 1.00 21.70 AAAA ATOM 1683 CZ TYR A 231 1.298 −7.729 − 13.281 1.00 21.49 AAAA ATOM 1684 OH TYR A 231 1.532 −6.662 − 12.466 1.00 18.68 AAAA ATOM 1685 C TYR A 231 0.047 −11.618 −18.285 1.00 28.10 AAAA ATOM 1686 O TYR A 231 0.834 − 11.249 − 19.163 1.00 27.39 AAAA ATOM 1687 N ALA A 232 −0.547 − 12.808 −18.297 1.00 28.86 AAAA ATOM 1688 CA ALA A 232 −0.310 − 13.775 − 19.364 1.00 29.80 AAAA ATOM 1689 CB ALA A 232 −1.013 − 15.091 − 19.046 1.00 30.32 AAAA ATOM 1690 C ALA A 232 −0.814 − 13.218 − 20.694 1.00 30.76 AAAA ATOM 1691 O ALA A 232 −0.147 − 13.336 −21.725 1.00 30.92 AAAA ATOM 1692 N GLU A 233 −1.996 − 12.614 − 20.662 1.00 31.01 AAAA ATOM 1693 CA GLU A 233 −2.592 − 12.034 −21.857 1.00 32.12 AAAA ATOM 1694 CB GLU A 233 −4.051 − 11.658 −21.579 1.00 33.81 AAAA ATOM 1695 CG GLU A 233 −4.975 − 12.871 −21.514 1.00 35.08 AAAA ATOM 1696 CD GLU A 233 −6.402 − 12.523 −21.117 1.00 37.70 AAAA ATOM 1697 OE1 GLU A 233 −6.875 − 11.419 −21.473 1.00 37.78 AAAA ATOM 1698 OE2 GLU A 233 −7.056 − 13.364 − 20.461 1.00 37.69 AAAA ATOM 1699 C GLU A 233 −1.800 − 10.820 −22.325 1.00 32.01 AAAA ATOM 1700 O GLU A 233 −1.825 − 10.463 −23.508 1.00 32.48 AAAA ATOM 1701 N ALA A 234 −1.093 − 10.185 −21.398 1.00 30.89 AAAA ATOM 1702 CA ALA A 234 −0.283 −9.022 −21.736 1.00 29.79 AAAA ATOM 1703 CB ALA A 234 −0.089 −8.141 −20.505 1.00 30.39 AAAA ATOM 1704 C ALA A 234 1.070 −9.501 −22.265 1.00 28.79 AAAA ATOM 1705 O ALA A 234 1.934 −8.697 −22.604 1.00 28.46 AAAA ATOM 1706 N GLY A 235 1.243 − 10.818 − 22.314 1.00 27.19 AAAA ATOM 1707 CA GLY A 235 2.484 − 11.388 −22.807 1.00 26.98 AAAA ATOM 1708 C GLY A 235 3.650 − 11.387 −21.832 1.00 25.89 AAAA ATOM 1709 O GLY A 235 4.798 −11.527 −22.253 1.00 25.26 AAAA ATOM 1710 N GLN A 236 3.370 − 11.226 − 20.540 1.00 24.71 AAAA ATOM 1711 CA GLN A 236 4.419 − 11.223 − 19.518 1.00 24.12 AAAA ATOM 1712 CB GLN A 236 4.652 −9.806 − 18.977 1.00 24.66 AAAA ATOM 1713 CG GLN A 236 5.116 −8.760 − 20.003 1.00 25.88 AAAA ATOM 1714 CD GLN A 236 6.454 −9.088 − 20.647 1.00 26.71 AAAA ATOM 1715 OE1 GLN A 236 7.410 −9.488 − 19.976 1.00 24.90 AAAA ATOM 1716 NE2 GLN A 236 6.533 −8.899 −21.960 1.00 26.33 AAAA ATOM 1717 C GLN A 236 3.959 − 12.132 − 18.379 1.00 22.79 AAAA ATOM 1718 O GLN A 236 3.823 − 11.696 − 17.233 1.00 22.19 AAAA ATOM 1719 N PRO A 237 3.740 − 13.419 − 18.679 1.00 22.50 AAAA ATOM 1720 CD PRO A 237 4.087 − 14.093 − 19.945 1.00 21.90 AAAA ATOM 1721 CA PRO A 237 3.282 − 14.395 − 17.684 1.00 22.78 AAAA ATOM 1722 CB PRO A 237 2.998 − 15.626 − 18.531 1.00 22.52 AAAA ATOM 1723 CG PRO A 237 4.105 − 15.558 − 19.543 1.00 23.54 AAAA ATOM 1724 C PRO A 237 4.252 − 14.695 − 16.550 1.00 22.53 AAAA ATOM 1725 O PRO A 237 3.845 − 15.217 − 15.512 1.00 23.09 AAAA ATOM 1726 N GLN A 238 5.521 − 14.346 − 16.735 1.00 22.30 AAAA ATOM 1727 CA GLN A 238 6.539 − 14.633 − 15.726 1.00 22.49 AAAA ATOM 1728 CB GLN A 238 7.947 − 14.437 − 16.304 1.00 22.24 AAAA ATOM 1729 CG GLN A 238 8.376 − 12.991 − 16.520 1.00 21.45 AAAA ATOM 1730 CD GLN A 238 7.727 − 12.356 − 17.736 1.00 22.77 AAAA ATOM 1731 OE1 GLN A 238 7.109 − 13.038 − 18.548 1.00 22.82 AAAA ATOM 1732 NE2 GLN A 238 7.881 − 11.046 − 17.870 1.00 22.96 AAAA ATOM 1733 C GLN A 238 6.453 − 13.856 − 14.426 1.00 21.84 AAAA ATOM 1734 O GLN A 238 7.059 − 14.253 − 13.427 1.00 21.75 AAAA ATOM 1735 N HIS A 239 5.724 − 12.748 − 14.420 1.00 22.21 AAAA ATOM 1736 CA HIS A 239 5.632 − 11.963 − 13.202 1.00 22.02 AAAA ATOM 1737 CB HIS A 239 4.919 − 10.638 − 13.479 1.00 22.03 AAAA ATOM 1738 CG HIS A 239 5.688 −9.734 − 14.392 1.00 22.30 AAAA ATOM 1739 CD2 HIS A 239 5.315 −9.057 − 15.505 1.00 22.95 AAAA ATOM 1740 ND1 HIS A 239 7.021 −9.445 − 14.197 1.00 21.95 AAAA ATOM 1741 CE1 HIS A 239 7.437 −8.628 − 15.149 1.00 23.56 AAAA ATOM 1742 NE2 HIS A 239 6.421 −8.378 − 15.956 1.00 21.89 AAAA ATOM 1743 C HIS A 239 4.937 − 12.739 − 12.092 1.00 20.83 AAAA ATOM 1744 O HIS A 239 4.036 − 13.538 − 12.352 1.00 21.43 AAAA ATOM 1745 N LYS A 240 5.381 − 12.506 − 10.858 1.00 21.17 AAAA ATOM 1746 CA LYS A 240 4.819 − 13.183 −9.687 1.00 22.02 AAAA ATOM 1747 CB LYS A 240 5.840 − 13.175 −8.543 1.00 21.72 AAAA ATOM 1748 CG LYS A 240 5.420 − 13.918 −7.257 1.00 22.71 AAAA ATOM 1749 CD LYS A 240 6.462 − 13.691 −6.163 1.00 23.02 AAAA ATOM 1750 CE LYS A 240 6.155 − 14.439 −4.855 1.00 22.89 AAAA ATOM 1751 NZ LYS A 240 6.359 − 15.920 −4.960 1.00 23.41 AAAA ATOM 1752 C LYS A 240 3.545 − 12.500 −9.214 1.00 21.50 AAAA ATOM 1753 O LYS A 240 3.527 − 11.288 −9.022 1.00 22.79 AAAA ATOM 1754 N VAL A 241 2.490 − 13.282 −9.012 1.00 23.27 AAAA ATOM 1755 CA VAL A 241 1.219 − 12.751 −8.527 1.00 23.82 AAAA ATOM 1756 CB VAL A 241 0.111 − 12.821 −9.598 1.00 23.97 AAAA ATOM 1757 CG1 VAL A 241 −1.170 − 12.185 −9.057 1.00 24.26 AAAA ATOM 1758 CG2 VAL A 241 0.563 − 12.105 − 10.862 1.00 22.10 AAAA ATOM 1759 C VAL A 241 0.751 − 13.565 −7.323 1.00 23.52 AAAA ATOM 1760 O VAL A 241 0.593 − 14.781 −7.415 1.00 25.10 AAAA ATOM 1761 N THR A 242 0.547 − 12.896 −6.195 1.00 24.29 AAAA ATOM 1762 CA THR A 242 0.083 − 13.578 −4.991 1.00 25.34 AAAA ATOM 1763 CB THR A 242 1.176 − 13.635 −3.892 1.00 23.46 AAAA ATOM 1764 OG1 THR A 242 1.633 − 12.312 −3.590 1.00 24.62 AAAA ATOM 1765 CG2 THR A 242 2.354 − 14.482 −4.351 1.00 25.33 AAAA ATOM 1766 C THR A 242 −1.144 − 12.870 −4.435 1.00 26.25 AAAA ATOM 1767 O THR A 242 −1.278 − 11.645 −4.534 1.00 25.29 AAAA ATOM 1768 N GLU A 243 −2.051 − 13.647 −3.860 1.00 26.45 AAAA ATOM 1769 CA GLU A 243 −3.256 − 13.070 −3.293 1.00 28.18 AAAA ATOM 1770 CB GLU A 243 −4.152 − 14.184 −2.746 1.00 28.90 AAAA ATOM 1771 CG GLU A 243 −5.463 − 13.705 −2.156 1.00 32.51 AAAA ATOM 1772 CD GLU A 243 −6.448 − 14.845 −1.957 1.00 33.27 AAAA ATOM 1773 OE1 GLU A 243 −6.002 − 15.969 −1.646 1.00 33.05 AAAA ATOM 1774 OE2 GLU A 243 −7.665 − 14.612 −2.107 1.00 34.89 AAAA ATOM 1775 C GLU A 243 −2.863 − 12.089 −2.194 1.00 27.96 AAAA ATOM 1776 O GLU A 243 −3.331 − 10.951 −2.164 1.00 28.25 AAAA ATOM 1777 N PHE A 244 −1.976 − 12.528 −1.308 1.00 28.29 AAAA ATOM 1778 CA PHE A 244 −1.509 − 11.696 −0.208 1.00 29.32 AAAA ATOM 1779 CB PHE A 244 −2.079 − 12.202 1.122 1.00 31.34 AAAA ATOM 1780 CG PHE A 244 −3.571 − 12.360 1.139 1.00 32.25 AAAA ATOM 1781 CD1 PHE A 244 −4.406 − 11.249 1.103 1.00 34.11 AAAA ATOM 1782 CD2 PHE A 244 −4.141 − 13.623 1.246 1.00 33.07 AAAA ATOM 1783 CE1 PHE A 244 −5.794 − 11.393 1.179 1.00 34.27 AAAA ATOM 1784 CE2 PHE A 244 −5.525 −13.780 1.323 1.00 34.74 AAAA ATOM 1785 CZ PHE A 244 −6.353 −12.660 1.291 1.00 34.28 AAAA ATOM 1786 C PHE A 244 0.010 − 11.759 −0.103 1.00 29.21 AAAA ATOM 1787 O PHE A 244 0.660 − 12.503 −0.836 1.00 28.44 AAAA ATOM 1788 N ILE A 245 0.560 − 10.962 0.813 1.00 29.58 AAAA ATOM 1789 CA ILE A 245 1.993 − 10.956 1.116 1.00 30.22 AAAA ATOM 1790 CB ILE A 245 2.764 −9.766 0.503 1.00 29.45 AAAA ATOM 1791 CG2 ILE A 245 4.190 −9.741 1.060 1.00 27.25 AAAA ATOM 1792 CG1 ILE A 245 2.824 −9.887 −1.020 1.00 26.11 AAAA ATOM 1793 CD1 ILE A 245 3.609 −8.774 −1.661 1.00 27.15 AAAA ATOM 1794 C ILE A 245 2.086 −10.822 2.631 1.00 32.52 AAAA ATOM 1795 O ILE A 245 1.987 −9.720 3.176 1.00 32.53 AAAA ATOM 1796 N ASP A 246 2.271 −11.944 3.311 1.00 34.55 AAAA ATOM 1797 CA ASP A 246 2.357 −11.926 4.763 1.00 36.92 AAAA ATOM 1798 CB ASP A 246 2.222 −13.350 5.304 1.00 40.29 AAAA ATOM 1799 CG ASP A 246 0.831 − 13.926 5.075 1.00 43.98 AAAA ATOM 1800 OD1 ASP A 246 0.659 − 15.159 5.218 1.00 46.68 AAAA ATOM 1801 OD2 ASP A 246 −0.093 13.143 4.760 1.00 45.65 AAAA ATOM 1802 C ASP A 246 3.650 − 11.286 5.247 1.00 36.42 AAAA ATOM 1803 O ASP A 246 3.631 − 10.384 6.092 1.00 37.48 AAAA ATOM 1804 N ASP A 247 4.771 − 11.733 4.694 1.00 35.16 AAAA ATOM 1805 CA ASP A 247 6.069 − 11.200 5.085 1.00 34.25 AAAA ATOM 1806 CB ASP A 247 7.145 − 12.268 4.887 1.00 33.07 AAAA ATOM 1807 CG ASP A 247 8.461 − 11.901 5.543 1.00 33.19 AAAA ATOM 1808 OD1 ASP A 247 8.689 − 10.700 5.802 1.00 31.85 AAAA ATOM 1809 OD2 ASP A 247 9.277 − 12.816 5.791 1.00 32.31 AAAA ATOM 1810 C ASP A 247 6.422 −9.949 4.275 1.00 34.18 AAAA ATOM 1811 O ASP A 247 7.241 − 10.003 3.354 1.00 33.62 AAAA ATOM 1812 N MET A 248 5.801 −8.825 4.617 1.00 33.66 AAAA ATOM 1813 CA MET A 248 6.069 −7.577 3.916 1.00 33.29 AAAA ATOM 1814 CB MET A 248 5.192 −6.448 4.461 1.00 34.30 AAAA ATOM 1815 CG MET A 248 3.852 −6.314 3.757 1.00 36.70 AAAA ATOM 1816 SD MET A 248 4.042 −5.940 1.987 1.00 40.22 AAAA ATOM 1817 CE MET A 248 2.590 −6.667 1.361 1.00 39.66 AAAA ATOM 1818 C MET A 248 7.533 −7.180 4.017 1.00 32.64 AAAA ATOM 1819 O MET A 248 8.082 −6.587 3.088 1.00 32.59 AAAA ATOM 1820 N ALA A 249 8.166 −7.500 5.142 1.00 30.31 AAAA ATOM 1821 CA ALA A 249 9.573 −7.163 5.316 1.00 29.81 AAAA ATOM 1822 CB ALA A 249 10.061 −7.597 6.706 1.00 28.83 AAAA ATOM 1823 C ALA A 249 10.406 −7.837 4.223 1.00 27.72 AAAA ATOM 1824 O ALA A 249 11.277 −7.208 3.622 1.00 27.98 AAAA ATOM 1825 N ALA A 250 10.127 −9.112 3.960 1.00 27.22 AAAA ATOM 1826 CA ALA A 250 10.858 −9.847 2.937 1.00 26.24 AAAA ATOM 1827 CB ALA A 250 10.449 −11.305 2.946 1.00 26.77 AAAA ATOM 1828 C ALA A 250 10.624 −9.250 1.553 1.00 26.35 AAAA ATOM 1829 O ALA A 250 11.543 −9.192 0.739 1.00 26.73 AAAA ATOM 1830 N ALA A 251 9.400 −8.807 1.279 1.00 25.03 AAAA ATOM 1831 CA ALA A 251 9.101 −8.225 −0.033 1.00 25.36 AAAA ATOM 1832 CB ALA A 251 7.597 −8.044 −0.205 1.00 24.69 AAAA ATOM 1833 C ALA A 251 9.816 −6.891 −0.209 1.00 24.97 AAAA ATOM 1834 O ALA A 251 10.342 −6.586 −1.287 1.00 24.32 AAAA ATOM 1835 N TYR A 252 9.832 −6.097 0.855 1.00 24.41 AAAA ATOM 1836 CA TYR A 252 10.488 −4.801 0.838 1.00 24.62 AAAA ATOM 1837 CB TYR A 252 10.191 −4.033 2.131 1.00 26.30 AAAA ATOM 1838 CG TYR A 252 8.815 −3.399 2.214 1.00 28.84 AAAA ATOM 1839 CD1 TYR A 252 8.282 −3.027 3.450 1.00 29.34 AAAA ATOM 1840 CE1 TYR A 252 7.048 −2.395 3.547 1.00 30.51 AAAA ATOM 1841 CD2 TYR A 252 8.066 −3.123 1.064 1.00 28.35 AAAA ATOM 1842 CE2 TYR A 252 6.821 −2.485 1.153 1.00 29.76 AAAA ATOM 1843 CZ TYR A 252 6.322 −2.125 2.401 1.00 30.32 AAAA ATOM 1844 OH TYR A 252 5.103 −1.492 2.515 1.00 29.75 AAAA ATOM 1845 C TYR A 252 11.998 −4.972 0.694 1.00 25.22 AAAA ATOM 1846 O TYR A 252 12.668 −4.106 0.139 1.00 24.57 AAAA ATOM 1847 N ALA A 253 12.527 −6.084 1.204 1.00 23.97 AAAA ATOM 1848 CA ALA A 253 13.961 −6.355 1.118 1.00 24.84 AAAA ATOM 1849 CB ALA A 253 14.311 −7.606 1.906 1.00 23.83 AAAA ATOM 1850 C ALA A 253 14.319 −6.560 −0.347 1.00 24.16 AAAA ATOM 1851 O ALA A 253 15.325 −6.045 −0.831 1.00 26.29 AAAA ATOM 1852 N TRP A 254 13.469 −7.315 −1.032 1.00 23.19 AAAA ATOM 1853 CA TRP A 254 13.640 −7.635 −2.447 1.00 22.89 AAAA ATOM 1854 CB TRP A 254 12.672 −8.753 −2.827 1.00 21.01 AAAA ATOM 1855 CG TRP A 254 12.534 −8.968 −4.304 1.00 21.21 AAAA ATOM 1856 CD2 TRP A 254 11.508 −8.437 −5.155 1.00 20.22 AAAA ATOM 1857 CE2 TRP A 254 11.766 −8.905 −6.463 1.00 20.36 AAAA ATOM 1858 CE3 TRP A 254 10.397 −7.610 −4.939 1.00 20.38 AAAA ATOM 1859 CD1 TRP A 254 13.353 −9.708 −5.105 1.00 20.80 AAAA ATOM 1860 NE1 TRP A 254 12.895 −9.678 −6.404 1.00 22.48 AAAA ATOM 1861 CZ2 TRP A 254 10.948 −8.573 −7.559 1.00 21.36 AAAA ATOM 1862 CZ3 TRP A 254 9.582 −7.276 −6.030 1.00 21.09 AAAA ATOM 1863 CH2 TRP A 254 9.867 −7.761 −7.323 1.00 20.78 AAAA ATOM 1864 C TRP A 254 13.433 −6.468 −3.414 1.00 22.65 AAAA ATOM 1865 O TRP A 254 14.218 −6.280 −4.345 1.00 23.19 AAAA ATOM 1866 N ALA A 255 12.376 −5.692 −3.194 1.00 21.49 AAAA ATOM 1867 CA ALA A 255 12.024 −4.586 −4.086 1.00 21.80 AAAA ATOM 1868 CB ALA A 255 10.652 −4.030 −3.677 1.00 22.15 AAAA ATOM 1869 C ALA A 255 12.988 −3.420 −4.299 1.00 21.27 AAAA ATOM 1870 O ALA A 255 13.844 −3.110 −3.469 1.00 21.35 AAAA ATOM 1871 N ASP A 256 12.820 −2.771 −5.447 1.00 21.80 AAAA ATOM 1872 CA ASP A 256 13.600 −1.590 −5.807 1.00 21.58 AAAA ATOM 1873 CB ASP A 256 14.082 −1.686 −7.263 1.00 23.50 AAAA ATOM 1874 CG ASP A 256 15.329 −2.542 −7.415 1.00 23.21 AAAA ATOM 1875 OD1 ASP A 256 15.354 −3.417 −8.306 1.00 24.63 AAAA ATOM 1876 OD2 ASP A 256 16.289 −2.328 −6.648 1.00 25.60 AAAA ATOM 1877 C ASP A 256 12.651 −0.397 −5.670 1.00 22.26 AAAA ATOM 1878 O ASP A 256 13.053 0.703 −5.300 1.00 22.77 AAAA ATOM 1879 N VAL A 257 11.379 −0.637 −5.968 1.00 23.20 AAAA ATOM 1880 CA VAL A 257 10.366 0.411 −5.914 1.00 23.31 AAAA ATOM 1881 CB VAL A 257 10.313 1.167 −7.267 1.00 23.63 AAAA ATOM 1882 CG1 VAL A 257 9.950 0.206 −8.373 1.00 21.70 AAAA ATOM 1883 CG2 VAL A 257 9.312 2.315 −7.205 1.00 23.86 AAAA ATOM 1884 C VAL A 257 8.997 −0.197 −5.607 1.00 23.39 AAAA ATOM 1885 O VAL A 257 8.735 −1.351 −5.933 1.00 22.20 AAAA ATOM 1886 N VAL A 258 8.127 0.587 −4.978 1.00 24.57 AAAA ATOM 1887 CA VAL A 258 6.792 0.114 −4.627 1.00 24.32 AAAA ATOM 1888 CB VAL A 258 6.590 0.100 −3.085 1.00 25.07 AAAA ATOM 1889 CG1 VAL A 258 5.275 −0.596 −2.731 1.00 25.09 AAAA ATOM 1890 CG2 VAL A 258 7.755 −0.599 −2.406 1.00 25.19 AAAA ATOM 1891 C VAL A 258 5.695 0.993 −5.228 1.00 24.77 AAAA ATOM 1892 O VAL A 258 5.806 2.220 −5.241 1.00 25.72 AAAA ATOM 1893 N VAL A 259 4.650 0.352 −5.738 1.00 24.90 AAAA ATOM 1894 CA VAL A 259 3.495 1.056 −6.291 1.00 24.40 AAAA ATOM 1895 CB VAL A 259 3.152 0.593 −7.713 1.00 24.26 AAAA ATOM 1896 CG1 VAL A 259 1.928 1.371 −8.226 1.00 22.17 AAAA ATOM 1897 CG2 VAL A 259 4.344 0.801 −8.628 1.00 21.85 AAAA ATOM 1898 C VAL A 259 2.351 0.653 −5.368 1.00 25.42 AAAA ATOM 1899 O VAL A 259 2.018 −0.528 −5.274 1.00 25.59 AAAA ATOM 1900 N CYS A 260 1.752 1.623 −4.685 1.00 25.57 AAAA ATOM 1901 CA CYS A 260 0.680 1.308 −3.750 1.00 26.61 AAAA ATOM 1902 CB CYS A 260 1.286 0.675 −2.495 1.00 25.90 AAAA ATOM 1903 SG CYS A 260 2.509 1.742 −1.683 1.00 29.42 AAAA ATOM 1904 C CYS A 260 −0.113 2.538 −3.330 1.00 27.15 AAAA ATOM 1905 O CYS A 260 0.221 3.664 −3.702 1.00 27.13 AAAA ATOM 1906 N ARG A 261 −1.164 2.306 −2.547 1.00 28.36 AAAA ATOM 1907 CA ARG A 261 −1.986 3.391 −2.023 1.00 29.99 AAAA ATOM 1908 CB ARG A 261 −3.244 2.848 −1.340 1.00 31.35 AAAA ATOM 1909 CG ARG A 261 −4.237 2.168 −2.258 1.00 33.82 AAAA ATOM 1910 CD ARG A 261 −4.829 3.143 −3.253 1.00 35.21 AAAA ATOM 1911 NE ARG A 261 −5.949 2.547 −3.975 1.00 36.21 AAAA ATOM 1912 CZ ARG A 261 −6.550 3.107 −5.017 1.00 36.46 AAAA ATOM 1913 NH1 ARG A 261 −6.138 4.283 −5.470 1.00 36.95 AAAA ATOM 1914 NH2 ARG A 261 − 7.571 2.493 −5.599 1.00 37.72 AAAA ATOM 1915 C ARG A 261 −1.118 4.076 −0.979 1.00 30.75 AAAA ATOM 1916 O ARG A 261 −0.041 3.575 −0.641 1.00 29.94 AAAA ATOM 1917 N SER A 262 −1.583 5.206 −0.453 1.00 30.70 AAAA ATOM 1918 CA SER A 262 −0.807 5.924 0.544 1.00 31.00 AAAA ATOM 1919 CB SER A 262 −0.290 7.245 −0.034 1.00 31.31 AAAA ATOM 1920 OG SER A 262 −1.344 8.016 −0.581 1.00 32.21 AAAA ATOM 1921 C SER A 262 −1.526 6.182 1.868 1.00 30.92 AAAA ATOM 1922 O SER A 262 −1.624 7.322 2.317 1.00 31.37 AAAA ATOM 1923 N GLY A 263 −2.040 5.121 2.483 1.00 30.70 AAAA ATOM 1924 CA GLY A 263 −2.669 5.277 3.779 1.00 29.85 AAAA ATOM 1925 C GLY A 263 −1.510 5.663 4.680 1.00 29.40 AAAA ATOM 1926 O GLY A 263 −0.367 5.287 4.394 1.00 28.65 AAAA ATOM 1927 N ALA A 264 −1.787 6.404 5.751 1.00 28.11 AAAA ATOM 1928 CA ALA A 264 −0.752 6.872 6.674 1.00 28.19 AAAA ATOM 1929 CB ALA A 264 −1.399 7.563 7.879 1.00 27.89 AAAA ATOM 1930 C ALA A 264 0.249 5.826 7.166 1.00 27.95 AAAA ATOM 1931 O ALA A 264 1.454 6.056 7.117 1.00 28.65 AAAA ATOM 1932 N LEU A 265 −0.239 4.693 7.656 1.00 27.93 AAAA ATOM 1933 CA LEU A 265 0.662 3.659 8.158 1.00 27.76 AAAA ATOM 1934 CB LEU A 265 −0.141 2.524 8.798 1.00 28.60 AAAA ATOM 1935 CG LEU A 265 −1.049 2.984 9.947 1.00 29.56 AAAA ATOM 1936 CD1 LEU A 265 −1.680 1.775 10.615 1.00 28.94 AAAA ATOM 1937 CD2 LEU A 265 −0.245 3.797 10.957 1.00 29.94 AAAA ATOM 1938 C LEU A 265 1.566 3.116 7.053 1.00 27.53 AAAA ATOM 1939 O LEU A 265 2.731 2.779 7.297 1.00 25.35 AAAA ATOM 1940 N THR A 266 1.026 3.043 5.841 1.00 27.19 AAAA ATOM 1941 CA THR A 266 1.778 2.553 4.689 1.00 27.20 AAAA ATOM 1942 CB THR A 266 0.859 2.383 3.455 1.00 27.48 AAAA ATOM 1943 OG1 THR A 266 −0.066 1.315 3.697 1.00 27.63 AAAA ATOM 1944 CG2 THR A 266 1.683 2.059 2.202 1.00 27.00 AAAA ATOM 1945 C THR A 266 2.916 3.507 4.341 1.00 27.11 AAAA ATOM 1946 O THR A 266 4.036 3.072 4.070 1.00 26.97 AAAA ATOM 1947 N VAL A 267 2.631 4.806 4.352 1.00 26.63 AAAA ATOM 1948 CA VAL A 267 3.649 5.806 4.048 1.00 27.06 AAAA ATOM 1949 CB VAL A 267 3.044 7.236 4.052 1.00 26.30 AAAA ATOM 1950 CG1 VAL A 267 4.146 8.289 4.011 1.00 26.39 AAAA ATOM 1951 CG2 VAL A 267 2.118 7.398 2.851 1.00 25.02 AAAA ATOM 1952 C VAL A 267 4.809 5.730 5.044 1.00 28.55 AAAA ATOM 1953 O VAL A 267 5.973 5.806 4.653 1.00 28.56 AAAA ATOM 1954 N SER A 268 4.495 5.581 6.329 1.00 28.38 AAAA ATOM 1955 CA SER A 268 5.537 5.492 7.351 1.00 29.48 AAAA ATOM 1956 CB SER A 268 4.915 5.522 8.753 1.00 29.48 AAAA ATOM 1957 OG SER A 268 4.291 6.768 9.003 1.00 30.64 AAAA ATOM 1958 C SER A 268 6.348 4.208 7.179 1.00 28.97 AAAA ATOM 1959 O SER A 268 7.557 4.181 7.399 1.00 30.06 AAAA ATOM 1960 N GLU A 269 5.663 3.146 6.785 1.00 28.87 AAAA ATOM 1961 CA GLU A 269 6.286 1.850 6.576 1.00 29.54 AAAA ATOM 1962 CB GLU A 269 5.189 0.821 6.328 1.00 29.82 AAAA ATOM 1963 CG GLU A 269 5.662 −0.594 6.185 1.00 31.86 AAAA ATOM 1964 CD GLU A 269 4.508 −1.562 6.155 1.00 31.85 AAAA ATOM 1965 OE1 GLU A 269 3.996 −1.917 7.239 1.00 32.48 AAAA ATOM 1966 OE2 GLU A 269 4.100 −1.956 5.048 1.00 30.84 AAAA ATOM 1967 C GLU A 269 7.263 1.910 5.394 1.00 29.59 AAAA ATOM 1968 O GLU A 269 8.355 1.332 5.441 1.00 29.11 AAAA ATOM 1969 N ILE A 270 6.867 2.616 4.340 1.00 27.88 AAAA ATOM 1970 CA ILE A 270 7.711 2.763 3.158 1.00 28.64 AAAA ATOM 1971 CB ILE A 270 6.968 3.520 2.028 1.00 28.20 AAAA ATOM 1972 CG2 ILE A 270 7.948 3.931 0.940 1.00 28.68 AAAA ATOM 1973 CG1 ILE A 270 5.845 2.646 1.461 1.00 28.04 AAAA ATOM 1974 CD1 ILE A 270 6.318 1.366 0.805 1.00 30.11 AAAA ATOM 1975 C ILE A 270 8.978 3.532 3.522 1.00 28.84 AAAA ATOM 1976 O ILE A 270 10.076 3.194 3.075 1.00 28.96 AAAA ATOM 1977 N ALA A 271 8.818 4.568 4.340 1.00 28.51 AAAA ATOM 1978 CA ALA A 271 9.952 5.374 4.768 1.00 28.79 AAAA ATOM 1979 CB ALA A 271 9.462 6.576 5.572 1.00 28.12 AAAA ATOM 1980 C ALA A 271 10.918 4.530 5.603 1.00 29.26 AAAA ATOM 1981 O ALA A 271 12.136 4.575 5.394 1.00 29.35 AAAA ATOM 1982 N ALA A 272 10.370 3.755 6.534 1.00 28.79 AAAA ATOM 1983 CA ALA A 272 11.187 2.904 7.397 1.00 29.79 AAAA ATOM 1984 CB ALA A 272 10.301 2.207 8.430 1.00 29.28 AAAA ATOM 1985 C ALA A 272 11.957 1.872 6.566 1.00 30.22 AAAA ATOM 1986 O ALA A 272 13.102 1.539 6.876 1.00 29.36 AAAA ATOM 1987 N ALA A 273 11.327 1.377 5.503 1.00 30.03 AAAA ATOM 1988 CA ALA A 273 11.961 0.394 4.628 1.00 30.65 AAAA ATOM 1989 CB ALA A 273 10.914 −0.306 3.782 1.00 29.48 AAAA ATOM 1990 C ALA A 273 13.005 1.041 3.720 1.00 31.45 AAAA ATOM 1991 O ALA A 273 13.803 0.346 3.090 1.00 31.87 AAAA ATOM 1992 N GLY A 274 12.998 2.368 3.662 1.00 31.20 AAAA ATOM 1993 CA GLY A 274 13.937 3.078 2.814 1.00 32.26 AAAA ATOM 1994 C GLY A 274 13.725 2.683 1.362 1.00 32.80 AAAA ATOM 1995 O GLY A 274 14.652 2.226 0.692 1.00 33.38 AAAA ATOM 1996 N LEU A 275 12.501 2.862 0.873 1.00 32.88 AAAA ATOM 1997 CA LEU A 275 12.169 2.494 −0.497 1.00 32.70 AAAA ATOM 1998 CB LEU A 275 11.266 1.262 −0.502 1.00 32.79 AAAA ATOM 1999 CG LEU A 275 11.869 −0.138 −0.431 1.00 33.70 AAAA ATOM 2000 CD1 LEU A 275 10.762 −1.133 −0.114 1.00 33.69 AAAA ATOM 2001 CD2 LEU A 275 12.538 −0.484 −1.762 1.00 32.25 AAAA ATOM 2002 C LEU A 275 11.479 3.568 −1.324 1.00 33.39 AAAA ATOM 2003 O LEU A 275 10.638 4.320 −0.819 1.00 32.48 AAAA ATOM 2004 N PRO A 276 11.835 3.654 −2.617 1.00 32.76 AAAA ATOM 2005 CD PRO A 276 13.022 3.048 −3.244 1.00 32.59 AAAA ATOM 2006 CA PRO A 276 11.221 4.636 −3.513 1.00 32.07 AAAA ATOM 2007 CB PRO A 276 12.049 4.510 −4.791 1.00 32.16 AAAA ATOM 2008 CG PRO A 276 13.383 4.072 −4.296 1.00 33.28 AAAA ATOM 2009 C PRO A 276 9.794 4.143 −3.722 1.00 31.63 AAAA ATOM 2010 O PRO A 276 9.531 2.936 −3.651 1.00 30.32 AAAA ATOM 2011 N ALA A 277 8.864 5.049 −3.976 1.00 31.27 AAAA ATOM 2012 CA ALA A 277 7.504 4.604 −4.180 1.00 30.99 AAAA ATOM 2013 CB ALA A 277 6.764 4.558 −2.842 1.00 30.75 AAAA ATOM 2014 C ALA A 277 6.722 5.450 −5.163 1.00 30.92 AAAA ATOM 2015 O ALA A 277 6.948 6.652 −5.295 1.00 32.61 AAAA ATOM 2016 N LEU A 278 5.809 4.796 −5.865 1.00 31.01 AAAA ATOM 2017 CA LEU A 278 4.928 5.476 −6.796 1.00 31.08 AAAA ATOM 2018 CB LEU A 278 4.884 4.758 −8.146 1.00 31.98 AAAA ATOM 2019 CG LEU A 278 4.135 5.526 −9.241 1.00 32.77 AAAA ATOM 2020 CD1 LEU A 278 4.770 6.895 −9.412 1.00 34.58 AAAA ATOM 2021 CD2 LEU A 278 4.181 4.756 −10.543 1.00 31.93 AAAA ATOM 2022 C LEU A 278 3.576 5.375 −6.101 1.00 30.98 AAAA ATOM 2023 O LEU A 278 2.887 4.357 −6.197 1.00 31.03 AAAA ATOM 2024 N PHE A 279 3.218 6.424 −5.369 1.00 30.84 AAAA ATOM 2025 CA PHE A 279 1.964 6.447 −4.633 1.00 29.87 AAAA ATOM 2026 CB PHE A 279 2.051 7.460 −3.489 1.00 29.31 AAAA ATOM 2027 CG PHE A 279 2.948 7.033 −2.353 1.00 26.86 AAAA ATOM 2028 CD1 PHE A 279 3.961 7.870 −1.902 1.00 27.25 AAAA ATOM 2029 CD2 PHE A 279 2.751 5.817 −1.710 1.00 26.40 AAAA ATOM 2030 CE1 PHE A 279 4.765 7.506 −0.821 1.00 27.90 AAAA ATOM 2031 CE2 PHE A 279 3.549 5.439 −0.630 1.00 25.57 AAAA ATOM 2032 CZ PHE A 279 4.555 6.286 −0.186 1.00 25.90 AAAA ATOM 2033 C PHE A 279 0.765 6.773 −5.508 1.00 30.70 AAAA ATOM 2034 O PHE A 279 0.790 7.719 −6.294 1.00 30.85 AAAA ATOM 2035 N VAL A 280 −0.281 5.968 −5.367 1.00 31.23 AAAA ATOM 2036 CA VAL A 280 −1.523 6.161 −6.101 1.00 32.57 AAAA ATOM 2037 CB VAL A 280 −1.867 4.924 −6.954 1.00 33.12 AAAA ATOM 2038 CG1 VAL A 280 −3.196 5.122 −7.661 1.00 32.63 AAAA ATOM 2039 CG2 VAL A 280 −0.768 4.688 −7.979 1.00 33.54 AAAA ATOM 2040 C VAL A 280 −2.598 6.394 −5.036 1.00 33.46 AAAA ATOM 2041 O VAL A 280 −3.320 5.478 −4.643 1.00 32.49 AAAA ATOM 2042 N PRO A 281 −2.695 7.640 −4.546 1.00 34.67 AAAA ATOM 2043 CD PRO A 281 −1.917 8.789 −5.036 1.00 34.47 AAAA ATOM 2044 CA PRO A 281 −3.652 8.061 −3.518 1.00 36.79 AAAA ATOM 2045 CB PRO A 281 −3.475 9.578 −3.478 1.00 36.20 AAAA ATOM 2046 CG PRO A 281 −2.060 9.772 −3.909 1.00 36.53 AAAA ATOM 2047 C PRO A 281 −5.097 7.676 −3.801 1.00 38.44 AAAA ATOM 2048 O PRO A 281 −5.564 7.763 −4.936 1.00 38.62 AAAA ATOM 2049 N PHE A 282 −5.800 7.237 −2.763 1.00 41.21 AAAA ATOM 2050 CA PHE A 282 −7.206 6.887 −2.910 1.00 44.31 AAAA ATOM 2051 CB PHE A 282 −7.722 6.169 −1.664 1.00 45.63 AAAA ATOM 2052 CG PHE A 282 −9.142 5.697 −1.785 1.00 47.68 AAAA ATOM 2053 CD1 PHE A 282 −9.452 4.570 −2.542 1.00 48.21 AAAA ATOM 2054 CD2 PHE A 282 −10.176 6.387 −1.156 1.00 48.55 AAAA ATOM 2055 CE1 PHE A 282 −10.772 4.136 −2.673 1.00 49.11 AAAA ATOM 2056 CE2 PHE A 282 −11.501 5.963 −1.280 1.00 49.07 AAAA ATOM 2057 CZ PHE A 282 −11.799 4.833 −2.041 1.00 48.80 AAAA ATOM 2058 C PHE A 282 −7.908 8.233 −3.052 1.00 45.26 AAAA ATOM 2059 O PHE A 282 −7.720 9.121 −2.224 1.00 45.48 AAAA ATOM 2060 N GLN A 283 −8.706 8.387 −4.101 1.00 47.00 AAAA ATOM 2061 CA GLN A 283 −9.399 9.648 −4.339 1.00 48.78 AAAA ATOM 2062 CB GLN A 283 −9.958 9.677 −5.768 1.00 48.98 AAAA ATOM 2063 CG GLN A 283 −10.606 11.000 −6.170 1.00 50.07 AAAA ATOM 2064 CD GLN A 283 −9.649 12.179 −6.082 1.00 50.05 AAAA ATOM 2065 OE1 GLN A 283 −9.206 12.556 −4.997 1.00 50.12 AAAA ATOM 2066 NE2 GLN A 283 −9.321 12.762 −7.230 1.00 50.62 AAAA ATOM 2067 C GLN A 283 −10.519 9.918 −3.335 1.00 49.60 AAAA ATOM 2068 O GLN A 283 −11.317 9.035 −3.018 1.00 49.68 AAAA ATOM 2069 N HIS A 284 −10.558 11.151 −2.838 1.00 50.76 AAAA ATOM 2070 CA HIS A 284 −11.570 11.579 −1.875 1.00 51.60 AAAA ATOM 2071 CB HIS A 284 −11.329 10.918 −0.515 1.00 52.12 AAAA ATOM 2072 CG HIS A 284 −12.436 11.140 0.469 1.00 52.63 AAAA ATOM 2073 CD2 HIS A 284 −13.327 10.280 1.017 1.00 52.98 AAAA ATOM 2074 ND1 HIS A 284 −12.733 12.381 0.991 1.00 52.98 AAAA ATOM 2075 CE1 HIS A 284 −13.758 12.276 1.817 1.00 52.69 AAAA ATOM 2076 NE2 HIS A 284 −14.138 11.011 1.851 1.00 52.96 AAAA ATOM 2077 C HIS A 284 −11.497 13.098 −1.745 1.00 52.04 AAAA ATOM 2078 O HIS A 284 −10.451 13.697 −2.000 1.00 52.03 AAAA ATOM 2079 N LYS A 285 −12.604 13.719 −1.347 1.00 52.27 AAAA ATOM 2080 CA LYS A 285 −12.653 15.171 −1.210 1.00 52.70 AAAA ATOM 2081 CB LYS A 285 −14.018 15.604 −0.669 1.00 53.61 AAAA ATOM 2082 CG LYS A 285 −14.256 17.111 −0.701 1.00 55.17 AAAA ATOM 2083 CD LYS A 285 −14.503 17.634 −2.122 1.00 56.00 AAAA ATOM 2084 CE LYS A 285 −13.244 17.625 −2.984 1.00 56.62 AAAA ATOM 2085 NZ LYS A 285 −13.513 18.075 −4.383 1.00 56.60 AAAA ATOM 2086 C LYS A 285 −11.552 15.746 −0.319 1.00 52.35 AAAA ATOM 2087 O LYS A 285 −10.988 16.800 −0.619 1.00 51.96 AAAA ATOM 2088 N ASP A 286 −11.246 15.054 0.773 1.00 51.71 AAAA ATOM 2089 CA ASP A 286 −10.218 15.521 1.693 1.00 51.34 AAAA ATOM 2090 CB ASP A 286 −10.405 14.869 3.067 1.00 53.33 AAAA ATOM 2091 CG ASP A 286 −10.003 13.403 3.083 1.00 55.00 AAAA ATOM 2092 OD1 ASP A 286 −10.412 12.648 2.174 1.00 56.57 AAAA ATOM 2093 OD2 ASP A 286 −9.280 13.004 4.018 1.00 56.62 AAAA ATOM 2094 C ASP A 286 −8.817 15.230 1.164 1.00 49.69 AAAA ATOM 2095 O ASP A 286 −7.840 15.829 1.616 1.00 49.71 AAAA ATOM 2096 N ARG A 287 −8.724 14.315 0.203 1.00 47.93 AAAA ATOM 2097 CA ARG A 287 −7.436 13.944 −0.380 1.00 45.79 AAAA ATOM 2098 CB ARG A 287 −6.848 15.121 −1.156 1.00 45.56 AAAA ATOM 2099 CG ARG A 287 −7.744 15.660 −2.251 1.00 45.87 AAAA ATOM 2100 CD ARG A 287 −7.172 16.949 −2.801 1.00 45.75 AAAA ATOM 2101 NE ARG A 287 −5.999 16.724 −3.637 1.00 46.20 AAAA ATOM 2102 CZ ARG A 287 −4.981 17.573 −3.733 1.00 46.22 AAAA ATOM 2103 NH1 ARG A 287 −4.986 18.702 −3.037 1.00 46.26 AAAA ATOM 2104 NH2 ARG A 287 −3.962 17.297 −4.533 1.00 46.42 AAAA ATOM 2105 C ARG A 287 −6.464 13.533 0.722 1.00 44.13 AAAA ATOM 2106 O ARG A 287 −5.279 13.870 0.685 1.00 43.87 AAAA ATOM 2107 N GLN A 288 −6.975 12.804 1.704 1.00 42.92 AAAA ATOM 2108 CA GLN A 288 −6.157 12.359 2.824 1.00 42.41 AAAA ATOM 2109 CB GLN A 288 −6.955 11.395 3.704 1.00 42.02 AAAA ATOM 2110 CG GLN A 288 −6.226 10.947 4.958 1.00 41.95 AAAA ATOM 2111 CD GLN A 288 −7.033 9.951 5.766 1.00 42.04 AAAA ATOM 2112 OE1 GLN A 288 −7.356 8.860 5.288 1.00 41.14 AAAA ATOM 2113 NE2 GLN A 288 −7.369 10.322 6.997 1.00 41.32 AAAA ATOM 2114 C GLN A 288 −4.867 11.682 2.372 1.00 41.36 AAAA ATOM 2115 O GLN A 288 −3.772 12.113 2.734 1.00 41.61 AAAA ATOM 2116 N GLN A 289 −4.999 10.626 1.575 1.00 41.32 AAAA ATOM 2117 CA GLN A 289 −3.835 9.886 1.105 1.00 40.21 AAAA ATOM 2118 CB GLN A 289 −4.267 8.678 0.280 1.00 39.57 AAAA ATOM 2119 CG GLN A 289 −5.126 7.703 1.068 1.00 37.69 AAAA ATOM 2120 CD GLN A 289 −4.976 6.274 0.595 1.00 37.80 AAAA ATOM 2121 OE1 GLN A 289 −4.422 6.014 −0.475 1.00 35.48 AAAA ATOM 2122 NE2 GLN A 289 −5.478 5.337 1.388 1.00 36.57 AAAA ATOM 2123 C GLN A 289 −2.862 10.744 0.318 1.00 40.38 AAAA ATOM 2124 O GLN A 289 −1.661 10.469 0.301 1.00 40.11 AAAA ATOM 2125 N TYR A 290 −3.373 11.782 −0.335 1.00 40.27 AAAA ATOM 2126 CA TYR A 290 −2.504 12.678 −1.081 1.00 39.93 AAAA ATOM 2127 CB TYR A 290 −3.316 13.715 −1.860 1.00 41.72 AAAA ATOM 2128 CG TYR A 290 −2.473 14.873 −2.352 1.00 43.41 AAAA ATOM 2129 CD1 TYR A 290 −1.590 14.716 −3.421 1.00 44.44 AAAA ATOM 2130 CE1 TYR A 290 −0.764 15.763 −3.836 1.00 45.65 AAAA ATOM 2131 CD2 TYR A 290 −2.513 16.109 −1.709 1.00 43.91 AAAA ATOM 2132 CE2 TYR A 290 −1.695 17.161 −2.111 1.00 45.19 AAAA ATOM 2133 CZ TYR A 290 −0.821 16.981 −3.174 1.00 46.54 AAAA ATOM 2134 OH TYR A 290 0.003 18.014 −3.566 1.00 47.98 AAAA ATOM 2135 C TYR A 290 −1.604 13.399 −0.085 1.00 39.33 AAAA ATOM 2136 O TYR A 290 −0.396 13.529 −0.296 1.00 39.19 AAAA ATOM 2137 N TRP A 291 −2.202 13.871 1.005 1.00 38.32 AAAA ATOM 2138 CA TRP A 291 −1.451 14.585 2.025 1.00 37.84 AAAA ATOM 2139 CB TRP A 291 −2.409 15.307 2.979 1.00 37.98 AAAA ATOM 2140 CG TRP A 291 −3.211 16.366 2.286 1.00 39.40 AAAA ATOM 2141 CD2 TRP A 291 −2.721 17.612 1.778 1.00 39.83 AAAA ATOM 2142 CE2 TRP A 291 −3.810 18.270 1.162 1.00 40.18 AAAA ATOM 2143 CE3 TRP A 291 −1.467 18.238 1.781 1.00 40.07 AAAA ATOM 2144 CD1 TRP A 291 −4.540 16.319 1.969 1.00 38.96 AAAA ATOM 2145 NE1 TRP A 291 −4.908 17.459 1.294 1.00 39.51 AAAA ATOM 2146 CZ2 TRP A 291 −3.684 19.525 0.554 1.00 40.53 AAAA ATOM 2147 CZ3 TRP A 291 −1.340 19.488 1.177 1.00 41.40 AAAA ATOM 2148 CH2 TRP A 291 −2.446 20.116 0.572 1.00 40.92 AAAA ATOM 2149 C TRP A 291 −0.506 13.680 2.803 1.00 36.79 AAAA ATOM 2150 O TRP A 291 0.515 14.141 3.306 1.00 36.64 AAAA ATOM 2151 N ASN A 292 −0.841 12.397 2.907 1.00 36.82 AAAA ATOM 2152 CA ASN A 292 0.030 11.467 3.619 1.00 37.08 AAAA ATOM 2153 CB ASN A 292 −0.658 10.116 3.842 1.00 36.47 AAAA ATOM 2154 CG ASN A 292 −1.841 10.203 4.783 1.00 36.02 AAAA ATOM 2155 OD1 ASN A 292 − 1.924 11.104 5.618 1.00 35.88 AAAA ATOM 2156 ND2 ASN A 292 −2.757 9.248 4.667 1.00 35.26 AAAA ATOM 2157 C ASN A 292 1.302 11.246 2.803 1.00 37.41 AAAA ATOM 2158 O ASN A 292 2.402 11.170 3.353 1.00 36.90 AAAA ATOM 2159 N ALA A 293 1.138 11.166 1.485 1.00 38.20 AAAA ATOM 2160 CA ALA A 293 2.253 10.936 0.567 1.00 38.64 AAAA ATOM 2161 CB ALA A 293 1.729 10.343 −0.737 1.00 37.83 AAAA ATOM 2162 C ALA A 293 3.085 12.176 0.267 1.00 39.51 AAAA ATOM 2163 O ALA A 293 4.311 12.094 0.158 1.00 39.51 AAAA ATOM 2164 N LEU A 294 2.422 13.321 0.137 1.00 40.40 AAAA ATOM 2165 CA LEU A 294 3.101 14.575 −0.169 1.00 40.96 AAAA ATOM 2166 CB LEU A 294 2.166 15.757 0.101 1.00 41.41 AAAA ATOM 2167 CG LEU A 294 2.666 17.155 −0.272 1.00 41.36 AAAA ATOM 2168 CD1 LEU A 294 3.231 17.168 −1.688 1.00 41.61 AAAA ATOM 2169 CD2 LEU A 294 1.510 18.136 −0.147 1.00 41.60 AAAA ATOM 2170 C LEU A 294 4.419 14.762 0.585 1.00 42.04 AAAA ATOM 2171 O LEU A 294 5.404 15.228 0.013 1.00 42.14 AAAA ATOM 2172 N PRO A 295 4.459 14.401 1.877 1.00 42.80 AAAA ATOM 2173 CD PRO A 295 3.351 14.022 2.772 1.00 42.95 AAAA ATOM 2174 CA PRO A 295 5.706 14.560 2.634 1.00 43.42 AAAA ATOM 2175 CB PRO A 295 5.336 14.032 4.015 1.00 43.51 AAAA ATOM 2176 CG PRO A 295 3.889 14.406 4.128 1.00 43.40 AAAA ATOM 2177 C PRO A 295 6.900 13.813 2.022 1.00 44.05 AAAA ATOM 2178 O PRO A 295 8.007 14.349 1.957 1.00 44.17 AAAA ATOM 2179 N LEU A 296 6.682 12.577 1.581 1.00 44.41 AAAA ATOM 2180 CA LEU A 296 7.766 11.800 0.980 1.00 45.13 AAAA ATOM 2181 CB LEU A 296 7.373 10.324 0.852 1.00 44.54 AAAA ATOM 2182 CG LEU A 296 7.424 9.484 2.130 1.00 44.46 AAAA ATOM 2183 CD1 LEU A 296 6.951 8.069 1.840 1.00 43.91 AAAA ATOM 2184 CD2 LEU A 296 8.844 9.469 2.667 1.00 44.76 AAAA ATOM 2185 C LEU A 296 8.151 12.346 −0.391 1.00 45.53 AAAA ATOM 2186 O LEU A 296 9.333 12.406 −0.732 1.00 45.28 AAAA ATOM 2187 N GLU A 297 7.155 12.747 −1.174 1.00 46.35 AAAA ATOM 2188 CA GLU A 297 7.421 13.291 −2.502 1.00 47.94 AAAA ATOM 2189 CB GLU A 297 6.113 13.563 −3.251 1.00 48.43 AAAA ATOM 2190 CG GLU A 297 6.306 14.349 −4.544 1.00 49.91 AAAA ATOM 2191 CD GLU A 297 5.014 14.543 −5.318 1.00 51.34 AAAA ATOM 2192 OE1 GLU A 297 4.562 13.586 −5.981 1.00 51.89 AAAA ATOM 2193 OE2 GLU A 297 4.446 15.655 −5.257 1.00 52.41 AAAA ATOM 2194 C GLU A 297 8.225 14.579 −2.393 1.00 48.46 AAAA ATOM 2195 O GLU A 297 9.155 14.806 −3.165 1.00 48.78 AAAA ATOM 2196 N LYS A 298 7.860 15.421 −1.431 1.00 49.07 AAAA ATOM 2197 CA LYS A 298 8.556 16.685 −1.226 1.00 49.76 AAAA ATOM 2198 CB LYS A 298 7.914 17.468 −0.077 1.00 50.85 AAAA ATOM 2199 CG LYS A 298 8.644 18.753 0.277 1.00 52.14 AAAA ATOM 2200 CD LYS A 298 8.032 19.429 1.492 1.00 53.44 AAAA ATOM 2201 CE LYS A 298 8.820 20.675 1.882 1.00 53.80 AAAA ATOM 2202 NZ LYS A 298 8.281 21.309 3.116 1.00 54.32 AAAA ATOM 2203 C LYS A 298 10.022 16.420 −0.908 1.00 49.36 AAAA ATOM 2204 O LYS A 298 10.904 17.180 −1.305 1.00 50.01 AAAA ATOM 2205 N ALA A 299 10.275 15.335 −0.138 1.00 48.67 AAAA ATOM 2206 CA ALA A 299 11.635 14.975 0.182 1.00 47.48 AAAA ATOM 2207 CB ALA A 299 11.615 14.001 1.353 1.00 47.29 AAAA ATOM 2208 C ALA A 299 12.354 14.356 −1.009 1.00 46.69 AAAA ATOM 2209 O ALA A 299 13.554 14.098 −0.953 1.00 46.67 AAAA ATOM 2210 N GLY A 300 11.613 14.133 −2.090 1.00 45.80 AAAA ATOM 2211 CA GLY A 300 12.197 13.538 −3.278 1.00 44.79 AAAA ATOM 2212 C GLY A 300 12.399 12.042 −3.119 1.00 44.04 AAAA ATOM 2213 O GLY A 300 13.343 11.472 −3.665 1.00 44.02 AAAA ATOM 2214 N ALA A 301 11.505 11.404 −2.370 1.00 43.01 AAAA ATOM 2215 CA ALA A 301 11.589 9.967 −2.131 1.00 42.10 AAAA ATOM 2216 CB ALA A 301 11.514 9.684 −0.632 1.00 42.10 AAAA ATOM 2217 C ALA A 301 10.484 9.209 −2.858 1.00 41.88 AAAA ATOM 2218 O ALA A 301 10.480 7.976 −2.882 1.00 41.48 AAAA ATOM 2219 N ALA A 302 9.549 9.941 −3.453 1.00 40.88 AAAA ATOM 2220 CA ALA A 302 8.451 9.303 −4.156 1.00 40.59 AAAA ATOM 2221 CB ALA A 302 7.411 8.818 −3.153 1.00 39.61 AAAA ATOM 2222 C ALA A 302 7.786 10.197 −5.191 1.00 40.72 AAAA ATOM 2223 O ALA A 302 8.123 11.372 −5.340 1.00 40.90 AAAA ATOM 2224 N LYS A 303 6.837 9.610 −5.910 1.00 41.39 AAAA ATOM 2225 CA LYS A 303 6.073 10.309 −6.930 1.00 41.79 AAAA ATOM 2226 CB LYS A 303 6.455 9.807 −8.325 1.00 41.86 AAAA ATOM 2227 CG LYS A 303 5.540 10.295 −9.442 1.00 43.46 AAAA ATOM 2228 CD LYS A 303 5.608 11.807 −9.614 1.00 44.98 AAAA ATOM 2229 CE LYS A 303 4.676 12.284 −10.729 1.00 46.33 AAAA ATOM 2230 NZ LYS A 303 4.767 13.759 −10.957 1.00 46.15 AAAA ATOM 2231 C LYS A 303 4.603 10.022 −6.671 1.00 41.86 AAAA ATOM 2232 O LYS A 303 4.219 8.873 −6.441 1.00 41.54 AAAA ATOM 2233 N ILE A 304 3.782 11.065 −6.702 1.00 41.98 AAAA ATOM 2234 CA ILE A 304 2.354 10.905 −6.475 1.00 42.52 AAAA ATOM 2235 CB ILE A 304 1.808 11.961 −5.492 1.00 42.27 AAAA ATOM 2236 CG2 ILE A 304 0.321 11.738 −5.278 1.00 41.77 AAAA ATOM 2237 CG1 ILE A 304 2.554 11.889 −4.159 1.00 42.76 AAAA ATOM 2238 CD1 ILE A 304 2.094 12.921 −3.140 1.00 41.84 AAAA ATOM 2239 C ILE A 304 1.580 11.047 −7.777 1.00 43.43 AAAA ATOM 2240 O ILE A 304 1.818 11.969 −8.555 1.00 43.89 AAAA ATOM 2241 N ILE A 305 0.649 10.129 −8.006 1.00 44.38 AAAA ATOM 2242 CA ILE A 305 −0.177 10.164 −9.199 1.00 45.28 AAAA ATOM 2243 CB ILE A 305 0.287 9.124 −10.247 1.00 44.81 AAAA ATOM 2244 CG2 ILE A 305 −0.610 9.188 −11.478 1.00 43.86 AAAA ATOM 2245 CG1 ILE A 305 1.738 9.400 −10.647 1.00 44.38 AAAA ATOM 2246 CD1 ILE A 305 2.305 8.405 −11.647 1.00 45.12 AAAA ATOM 2247 C ILE A 305 −1.620 9.870 −8.807 1.00 47.13 AAAA ATOM 2248 O ILE A 305 −1.985 8.724 −8.550 1.00 46.47 AAAA ATOM 2249 N GLU A 306 −2.435 10.918 −8.745 1.00 49.50 AAAA ATOM 2250 CA GLU A 306 −3.839 10.761 −8.396 1.00 51.69 AAAA ATOM 2251 CB GLU A 306 −4.430 12.110 −7.987 1.00 51.85 AAAA ATOM 2252 CG GLU A 306 −3.603 12.818 −6.927 1.00 51.67 AAAA ATOM 2253 CD GLU A 306 −4.324 13.990 −6.296 1.00 52.25 AAAA ATOM 2254 OE1 GLU A 306 −5.351 13.763 −5.621 1.00 52.52 AAAA ATOM 2255 OE2 GLU A 306 − 3.861 15.135 −6.472 1.00 52.12 AAAA ATOM 2256 C GLU A 306 −4.552 10.202 −9.619 1.00 53.21 AAAA ATOM 2257 O GLU A 306 −4.180 10.515 −10.749 1.00 53.53 AAAA ATOM 2258 N GLN A 307 −5.570 9.376 −9.393 1.00 55.39 AAAA ATOM 2259 CA GLN A 307 −6.313 8.750 −10.483 1.00 57.63 AAAA ATOM 2260 CB GLN A 307 −7.553 8.035 −9.934 1.00 58.22 AAAA ATOM 2261 CG GLN A 307 −7.213 6.925 −8.937 1.00 59.17 AAAA ATOM 2262 CD GLN A 307 −8.196 5.766 −8.970 1.00 59.83 AAAA ATOM 2263 OE1 GLN A 307 −8.110 4.840 −8.160 1.00 60.26 AAAA ATOM 2264 NE2 GLN A 307 −9.131 5.807 −9.912 1.00 60.69 AAAA ATOM 2265 C GLN A 307 −6.703 9.663 −11.648 1.00 58.47 AAAA ATOM 2266 O GLN A 307 −6.774 9.208 −12.791 1.00 58.81 AAAA ATOM 2267 N PRO A 308 −6.968 10.956 −11.385 1.00 59.24 AAAA ATOM 2268 CD PRO A 308 −7.113 11.674 −10.105 1.00 59.76 AAAA ATOM 2269 CA PRO A 308 −7.334 11.825 −12.507 1.00 59.72 AAAA ATOM 2270 CB PRO A 308 −7.360 13.209 −11.870 1.00 59.96 AAAA ATOM 2271 CG PRO A 308 −7.896 12.914 −10.510 1.00 60.00 AAAA ATOM 2272 C PRO A 308 −6.318 11.723 −13.641 1.00 59.84 AAAA ATOM 2273 O PRO A 308 −6.685 11.496 −14.795 1.00 60.34 AAAA ATOM 2274 N GLN A 309 −5.042 11.881 −13.305 1.00 59.45 AAAA ATOM 2275 CA GLN A 309 −3.985 11.794 −14.303 1.00 58.69 AAAA ATOM 2276 CB GLN A 309 −2.992 12.947 −14.135 1.00 59.92 AAAA ATOM 2277 CG GLN A 309 −2.082 12.838 −12.920 1.00 60.97 AAAA ATOM 2278 CD GLN A 309 −1.077 13.975 −12.843 1.00 61.96 AAAA ATOM 2279 OE1 GLN A 309 −0.180 13.974 −11.997 1.00 62.79 AAAA ATOM 2280 NE2 GLN A 309 −1.226 14.956 −13.728 1.00 62.49 AAAA ATOM 2281 C GLN A 309 −3.250 10.459 −14.204 1.00 57.53 AAAA ATOM 2282 O GLN A 309 −2.078 10.358 −14.567 1.00 57.67 AAAA ATOM 2283 N LEU A 310 −3.947 9.437 −13.711 1.00 55.75 AAAA ATOM 2284 CA LEU A 310 −3.364 8.107 −13.570 1.00 53.92 AAAA ATOM 2285 CB LEU A 310 −3.799 7.473 −12.241 1.00 53.77 AAAA ATOM 2286 CG LEU A 310 −3.242 6.108 −11.804 1.00 53.75 AAAA ATOM 2287 CD1 LEU A 310 −3.810 4.998 −12.669 1.00 54.14 AAAA ATOM 2288 CD2 LEU A 310 −1.727 6.123 −11.876 1.00 52.88 AAAA ATOM 2289 C LEU A 310 −3.813 7.243 −14.740 1.00 52.48 AAAA ATOM 2290 O LEU A 310 −5.003 7.162 −15.044 1.00 53.10 AAAA ATOM 2291 N SER A 311 −2.852 6.603 −15.395 1.00 49.96 AAAA ATOM 2292 CA SER A 311 −3.136 5.748 −16.540 1.00 47.96 AAAA ATOM 2293 CB SER A 311 −3.409 6.599 −17.778 1.00 47.62 AAAA ATOM 2294 OG SER A 311 −2.232 7.287 −18.168 1.00 46.72 AAAA ATOM 2295 C SER A 311 −1.936 4.849 −16.815 1.00 46.16 AAAA ATOM 2296 O SER A 311 −0.873 5.018 −16.212 1.00 45.34 AAAA ATOM 2297 N VAL A 312 −2.113 3.907 −17.736 1.00 44.77 AAAA ATOM 2298 CA VAL A 312 −1.056 2.972 −18.103 1.00 43.52 AAAA ATOM 2299 CB VAL A 312 −1.496 2.066 −19.278 1.00 43.96 AAAA ATOM 2300 CG1 VAL A 312 −0.373 1.112 −19.656 1.00 43.81 AAAA ATOM 2301 CG2 VAL A 312 −2.740 1.285 −18.892 1.00 43.95 AAAA ATOM 2302 C VAL A 312 0.215 3.712 −18.498 1.00 42.79 AAAA ATOM 2303 O VAL A 312 1.284 3.488 −17.922 1.00 41.92 AAAA ATOM 2304 N ASP A 313 0.096 4.610 −19.470 1.00 42.00 AAAA ATOM 2305 CA ASP A 313 1.252 5.364 −19.939 1.00 41.37 AAAA ATOM 2306 CB ASP A 313 0.877 6.203 −21.163 1.00 43.96 AAAA ATOM 2307 CG ASP A 313 0.506 5.345 −22.357 1.00 46.32 AAAA ATOM 2308 OD1 ASP A 313 1.334 4.496 −22.755 1.00 47.81 AAAA ATOM 2309 OD2 ASP A 313 −0.610 5.514 −22.896 1.00 48.38 AAAA ATOM 2310 C ASP A 313 1.856 6.249 −18.864 1.00 39.53 AAAA ATOM 2311 O ASP A 313 3.069 6.452 −18.832 1.00 39.95 AAAA ATOM 2312 N ALA A 314 1.015 6.768 −17.978 1.00 38.08 AAAA ATOM 2313 CA ALA A 314 1.492 7.629 −16.905 1.00 36.44 AAAA ATOM 2314 CB ALA A 314 0.306 8.233 −16.156 1.00 36.79 AAAA ATOM 2315 C ALA A 314 2.382 6.844 −15.939 1.00 35.41 AAAA ATOM 2316 O ALA A 314 3.448 7.313 −15.535 1.00 35.44 AAAA ATOM 2317 N VAL A 315 1.940 5.648 −15.569 1.00 34.29 AAAA ATOM 2318 CA VAL A 315 2.708 4.809 −14.652 1.00 33.44 AAAA ATOM 2319 CB VAL A 315 1.886 3.592 −14.169 1.00 33.40 AAAA ATOM 2320 CG1 VAL A 315 2.707 2.775 −13.180 1.00 33.12 AAAA ATOM 2321 CG2 VAL A 315 0.588 4.059 −13.521 1.00 32.76 AAAA ATOM 2322 C VAL A 315 3.970 4.295 −15.328 1.00 32.88 AAAA ATOM 2323 O VAL A 315 5.071 4.426 −14.792 1.00 32.35 AAAA ATOM 2324 N ALA A 316 3.805 3.708 −16.508 1.00 33.02 AAAA ATOM 2325 CA ALA A 316 4.940 3.172 −17.250 1.00 34.17 AAAA ATOM 2326 CB ALA A 316 4.469 2.616 −18.593 1.00 33.68 AAAA ATOM 2327 C ALA A 316 6.002 4.252 −17.456 1.00 34.75 AAAA ATOM 2328 O ALA A 316 7.190 4.026 −17.211 1.00 34.70 AAAA ATOM 2329 N ASN A 317 5.578 5.434 −17.889 1.00 35.49 AAAA ATOM 2330 CA ASN A 317 6.524 6.518 −18.108 1.00 35.27 AAAA ATOM 2331 CB ASN A 317 5.815 7.738 −18.694 1.00 37.74 AAAA ATOM 2332 CG ASN A 317 5.395 7.518 −20.128 1.00 38.86 AAAA ATOM 2333 OD1 ASN A 317 6.099 6.855 −20.889 1.00 39.80 AAAA ATOM 2334 ND2 ASN A 317 4.252 8.077 −20.511 1.00 40.96 AAAA ATOM 2335 C ASN A 317 7.272 6.916 −16.847 1.00 35.18 AAAA ATOM 2336 O ASN A 317 8.458 7.239 −16.904 1.00 34.36 AAAA ATOM 2337 N THR A 318 6.592 6.891 −15.704 1.00 34.31 AAAA ATOM 2338 CA THR A 318 7.251 7.262 −14.456 1.00 34.35 AAAA ATOM 2339 CB THR A 318 6.245 7.358 −13.282 1.00 34.55 AAAA ATOM 2340 OG1 THR A 318 5.353 8.460 −13.498 1.00 34.46 AAAA ATOM 2341 CG2 THR A 318 6.984 7.568 −11.969 1.00 34.42 AAAA ATOM 2342 C THR A 318 8.335 6.252 −14.093 1.00 34.52 AAAA ATOM 2343 O THR A 318 9.464 6.624 −13.783 1.00 34.11 AAAA ATOM 2344 N LEU A 319 7.987 4.971 −14.139 1.00 35.35 AAAA ATOM 2345 CA LEU A 319 8.937 3.918 −13.801 1.00 35.23 AAAA ATOM 2346 CB LEU A 319 8.233 2.556 −13.804 1.00 34.91 AAAA ATOM 2347 CG LEU A 319 7.142 2.362 −12.743 1.00 34.50 AAAA ATOM 2348 CD1 LEU A 319 6.445 1.031 −12.956 1.00 34.48 AAAA ATOM 2349 CD2 LEU A 319 7.761 2.432 −11.351 1.00 35.13 AAAA ATOM 2350 C LEU A 319 10.107 3.907 −14.777 1.00 35.72 AAAA ATOM 2351 O LEU A 319 11.264 3.830 −14.370 1.00 34.85 AAAA ATOM 2352 N ALA A 320 9.801 3.997 −16.067 1.00 36.49 AAAA ATOM 2353 CA ALA A 320 10.832 3.989 −17.096 1.00 38.10 AAAA ATOM 2354 CB ALA A 320 10.192 4.051 −18.472 1.00 37.58 AAAA ATOM 2355 C ALA A 320 11.809 5.144 −16.924 1.00 38.94 AAAA ATOM 2356 O ALA A 320 12.939 5.087 −17.410 1.00 39.51 AAAA ATOM 2357 N GLY A 321 11.375 6.186 −16.219 1.00 38.88 AAAA ATOM 2358 CA GLY A 321 12.224 7.347 −16.013 1.00 38.68 AAAA ATOM 2359 C GLY A 321 13.117 7.303 −14.788 1.00 38.70 AAAA ATOM 2360 O GLY A 321 13.881 8.235 −14.542 1.00 38.64 AAAA ATOM 2361 N TRP A 322 13.028 6.230 −14.010 1.00 38.46 AAAA ATOM 2362 CA TRP A 322 13.855 6.108 −12.820 1.00 38.53 AAAA ATOM 2363 CB TRP A 322 13.008 5.688 −11.611 1.00 39.41 AAAA ATOM 2364 CG TRP A 322 12.047 6.748 −11.146 1.00 40.01 AAAA ATOM 2365 CD2 TRP A 322 10.898 6.558 −10.307 1.00 40.49 AAAA ATOM 2366 CE2 TRP A 322 10.330 7.833 −10.081 1.00 41.27 AAAA ATOM 2367 CE3 TRP A 322 10.295 5.436 −9.722 1.00 40.54 AAAA ATOM 2368 CD1 TRP A 322 12.126 8.091 −11.389 1.00 39.97 AAAA ATOM 2369 NE1 TRP A 322 11.098 8.749 −10.752 1.00 40.69 AAAA ATOM 2370 CZ2 TRP A 322 9.186 8.018 −9.293 1.00 41.67 AAAA ATOM 2371 CZ3 TRP A 322 9.155 5.619 −8.938 1.00 41.40 AAAA ATOM 2372 CH2 TRP A 322 8.615 6.903 −8.732 1.00 41.69 AAAA ATOM 2373 C TRP A 322 14.984 5.109 −13.027 1.00 38.48 AAAA ATOM 2374 O TRP A 322 14.743 3.929 −13.271 1.00 38.22 AAAA ATOM 2375 N SER A 323 16.217 5.596 −12.935 1.00 38.13 AAAA ATOM 2376 CA SER A 323 17.395 4.753 −13.101 1.00 38.51 AAAA ATOM 2377 CB SER A 323 18.573 5.590 −13.591 1.00 38.51 AAAA ATOM 2378 OG SER A 323 18.994 6.489 −12.582 1.00 39.52 AAAA ATOM 2379 C SER A 323 17.739 4.150 −11.744 1.00 38.37 AAAA ATOM 2380 O SER A 323 17.188 4.566 −10.725 1.00 37.29 AAAA ATOM 2381 N ARG A 324 18.647 3.178 −11.723 1.00 37.86 AAAA ATOM 2382 CA ARG A 324 19.030 2.563 −10.461 1.00 37.82 AAAA ATOM 2383 CB ARG A 324 19.924 1.341 −10.688 1.00 36.36 AAAA ATOM 2384 CG ARG A 324 19.130 0.077 −10.959 1.00 34.77 AAAA ATOM 2385 CD ARG A 324 19.978 −1.176 −10.849 1.00 33.04 AAAA ATOM 2386 NE ARG A 324 19.143 −2.372 −10.888 1.00 31.23 AAAA ATOM 2387 CZ ARG A 324 18.318 −2.738 −9.908 1.00 29.95 AAAA ATOM 2388 NH1 ARG A 324 18.228 −2.006 −8.808 1.00 28.46 AAAA ATOM 2389 NH2 ARG A 324 17.562 −3.815 −10.041 1.00 28.17 AAAA ATOM 2390 C ARG A 324 19.731 3.571 −9.569 1.00 38.78 AAAA ATOM 2391 O ARG A 324 19.532 3.578 −8.354 1.00 38.12 AAAA ATOM 2392 N GLU A 325 20.551 4.428 −10.169 1.00 39.55 AAAA ATOM 2393 CA GLU A 325 21.251 5.447 −9.401 1.00 40.60 AAAA ATOM 2394 CB GLU A 325 22.208 6.236 −10.304 1.00 42.74 AAAA ATOM 2395 CG GLU A 325 22.642 7.589 −9.745 1.00 46.19 AAAA ATOM 2396 CD GLU A 325 23.197 7.517 −8.327 1.00 48.10 AAAA ATOM 2397 OE1 GLU A 325 23.535 8.586 −7.770 1.00 49.61 AAAA ATOM 2398 OE2 GLU A 325 23.297 6.403 −7.768 1.00 49.87 AAAA ATOM 2399 C GLU A 325 20.214 6.380 −8.784 1.00 39.88 AAAA ATOM 2400 O GLU A 325 20.324 6.771 −7.623 1.00 39.45 AAAA ATOM 2401 N THR A 326 19.202 6.725 −9.572 1.00 39.89 AAAA ATOM 2402 CA THR A 326 18.130 7.591 −9.102 1.00 40.25 AAAA ATOM 2403 CB THR A 326 17.139 7.912 −10.240 1.00 40.72 AAAA ATOM 2404 OG1 THR A 326 17.828 8.593 −11.298 1.00 42.28 AAAA ATOM 2405 CG2 THR A 326 16.006 8.795 −9.730 1.00 41.64 AAAA ATOM 2406 C THR A 326 17.371 6.897 −7.968 1.00 39.76 AAAA ATOM 2407 O THR A 326 17.108 7.497 −6.925 1.00 39.87 AAAA ATOM 2408 N LEU A 327 17.027 5.628 −8.175 1.00 38.46 AAAA ATOM 2409 CA LEU A 327 16.294 4.867 −7.169 1.00 37.41 AAAA ATOM 2410 CB LEU A 327 15.968 3.466 −7.697 1.00 36.19 AAAA ATOM 2411 CG LEU A 327 14.952 3.426 −8.843 1.00 35.32 AAAA ATOM 2412 CD1 LEU A 327 14.802 2.002 −9.370 1.00 35.07 AAAA ATOM 2413 CD2 LEU A 327 13.614 3.961 −8.354 1.00 34.69 AAAA ATOM 2414 C LEU A 327 17.050 4.774 −5.845 1.00 37.39 AAAA ATOM 2415 O LEU A 327 16.437 4.807 −4.778 1.00 36.80 AAAA ATOM 2416 N LEU A 328 18.375 4.665 −5.909 1.00 37.58 AAAA ATOM 2417 CA LEU A 328 19.184 4.593 −4.693 1.00 38.35 AAAA ATOM 2418 CB LEU A 328 20.662 4.368 −5.030 1.00 38.95 AAAA ATOM 2419 CG LEU A 328 21.636 4.544 −3.854 1.00 40.10 AAAA ATOM 2420 CD1 LEU A 328 21.303 3.551 −2.752 1.00 39.51 AAAA ATOM 2421 CD2 LEU A 328 23.068 4.349 −4.330 1.00 40.30 AAAA ATOM 2422 C LEU A 328 19.039 5.899 −3.926 1.00 38.68 AAAA ATOM 2423 O LEU A 328 18.929 5.906 −2.697 1.00 38.65 AAAA ATOM 2424 N THR A 329 19.048 7.004 −4.664 1.00 39.35 AAAA ATOM 2425 CA THR A 329 18.908 8.326 −4.068 1.00 39.98 AAAA ATOM 2426 CB THR A 329 19.002 9.433 −5.136 1.00 40.05 AAAA ATOM 2427 OG1 THR A 329 20.280 9.364 −5.782 1.00 41.54 AAAA ATOM 2428 CG2 THR A 329 18.841 10.808 −4.497 1.00 40.35 AAAA ATOM 2429 C THR A 329 17.557 8.425 −3.367 1.00 39.68 AAAA ATOM 2430 O THR A 329 17.485 8.743 −2.179 1.00 39.91 AAAA ATOM 2431 N MET A 330 16.492 8.147 −4.111 1.00 39.51 AAAA ATOM 2432 CA MET A 330 15.143 8.190 −3.564 1.00 38.79 AAAA ATOM 2433 CB MET A 330 14.141 7.718 −4.617 1.00 38.09 AAAA ATOM 2434 CG MET A 330 14.011 8.657 −5.804 1.00 36.84 AAAA ATOM 2435 SD MET A 330 12.977 7.980 −7.108 1.00 37.95 AAAA ATOM 2436 CE MET A 330 11.332 8.342 −6.478 1.00 37.58 AAAA ATOM 2437 C MET A 330 15.037 7.315 −2.319 1.00 39.71 AAAA ATOM 2438 O MET A 330 14.418 7.703 −1.326 1.00 39.60 AAAA ATOM 2439 N ALA A 331 15.646 6.135 −2.381 1.00 39.50 AAAA ATOM 2440 CA ALA A 331 15.625 5.202 −1.266 1.00 40.36 AAAA ATOM 2441 CB ALA A 331 16.378 3.928 −1.634 1.00 39.91 AAAA ATOM 2442 C ALA A 331 16.243 5.843 −0.032 1.00 40.98 AAAA ATOM 2443 O ALA A 331 15.662 5.805 1.052 1.00 40.34 AAAA ATOM 2444 N GLU A 332 17.422 6.435 −0.201 1.00 41.85 AAAA ATOM 2445 CA GLU A 332 18.102 7.087 0.911 1.00 42.77 AAAA ATOM 2446 CB GLU A 332 19.470 7.607 0.465 1.00 44.04 AAAA ATOM 2447 CG GLU A 332 20.414 6.500 0.016 1.00 46.55 AAAA ATOM 2448 CD GLU A 332 21.822 6.994 −0.248 1.00 48.04 AAAA ATOM 2449 OE1 GLU A 332 21.981 7.923 −1.065 1.00 49.87 AAAA ATOM 2450 OE2 GLU A 332 22.770 6.449 0.359 1.00 49.38 AAAA ATOM 2451 C GLU A 332 17.246 8.228 1.445 1.00 42.38 AAAA ATOM 2452 O GLU A 332 17.156 8.435 2.653 1.00 42.66 AAAA ATOM 2453 N ARG A 333 16.619 8.969 0.540 1.00 41.80 AAAA ATOM 2454 CA ARG A 333 15.752 10.067 0.937 1.00 42.25 AAAA ATOM 2455 CB ARG A 333 15.212 10.784 −0.306 1.00 43.43 AAAA ATOM 2456 CG ARG A 333 16.184 11.793 −0.926 1.00 45.99 AAAA ATOM 2457 CD ARG A 333 15.844 12.060 −2.389 1.00 48.51 AAAA ATOM 2458 NE ARG A 333 16.415 13.301 −2.913 1.00 50.45 AAAA ATOM 2459 CZ ARG A 333 17.703 13.631 −2.859 1.00 52.07 AAAA ATOM 2460 NH1 ARG A 333 18.585 12.814 −2.297 1.00 52.45 AAAA ATOM 2461 NH2 ARG A 333 18.112 14.784 −3.377 1.00 51.94 AAAA ATOM 2462 C ARG A 333 14.594 9.519 1.777 1.00 41.39 AAAA ATOM 2463 O ARG A 333 14.275 10.060 2.834 1.00 40.21 AAAA ATOM 2464 N ALA A 334 13.981 8.435 1.308 1.00 40.03 AAAA ATOM 2465 CA ALA A 334 12.859 7.825 2.014 1.00 39.84 AAAA ATOM 2466 CB ALA A 334 12.356 6.612 1.241 1.00 38.43 AAAA ATOM 2467 C ALA A 334 13.239 7.417 3.435 1.00 40.05 AAAA ATOM 2468 O ALA A 334 12.493 7.665 4.386 1.00 40.41 AAAA ATOM 2469 N ARG A 335 14.404 6.797 3.577 1.00 39.11 AAAA ATOM 2470 CA ARG A 335 14.874 6.351 4.881 1.00 40.00 AAAA ATOM 2471 CB ARG A 335 16.137 5.506 4.719 1.00 39.98 AAAA ATOM 2472 CG ARG A 335 16.631 4.865 6.000 1.00 40.54 AAAA ATOM 2473 CD ARG A 335 15.653 3.814 6.501 1.00 42.08 AAAA ATOM 2474 NE ARG A 335 16.263 2.949 7.507 1.00 42.95 AAAA ATOM 2475 CZ ARG A 335 16.403 1.634 7.373 1.00 43.43 AAAA ATOM 2476 NH1 ARG A 335 15.972 1.024 6.274 1.00 43.17 AAAA ATOM 2477 NH2 ARG A 335 16.983 0.927 8.335 1.00 43.96 AAAA ATOM 2478 C ARG A 335 15.167 7.527 5.802 1.00 40.09 AAAA ATOM 2479 O ARG A 335 14.877 7.479 6.997 1.00 39.35 AAAA ATOM 2480 N ALA A 336 15.745 8.581 5.237 1.00 40.52 AAAA ATOM 2481 CA ALA A 336 16.089 9.774 6.001 1.00 41.50 AAAA ATOM 2482 CB ALA A 336 16.850 10.754 5.116 1.00 41.05 AAAA ATOM 2483 C ALA A 336 14.847 10.447 6.573 1.00 42.00 AAAA ATOM 2484 O ALA A 336 14.905 11.087 7.621 1.00 42.49 AAAA ATOM 2485 N ALA A 337 13.725 10.300 5.879 1.00 42.58 AAAA ATOM 2486 CA ALA A 337 12.475 10.903 6.320 1.00 42.55 AAAA ATOM 2487 CB ALA A 337 11.656 11.338 5.111 1.00 42.34 AAAA ATOM 2488 C ALA A 337 11.670 9.932 7.174 1.00 42.43 AAAA ATOM 2489 O ALA A 337 10.444 10.000 7.209 1.00 44.01 AAAA ATOM 2490 N SER A 338 12.360 9.035 7.868 1.00 41.93 AAAA ATOM 2491 CA SER A 338 11.686 8.053 8.708 1.00 41.12 AAAA ATOM 2492 CB SER A 338 12.097 6.641 8.293 1.00 40.73 AAAA ATOM 2493 OG SER A 338 11.504 5.671 9.139 1.00 40.32 AAAA ATOM 2494 C SER A 338 11.964 8.235 10.198 1.00 40.88 AAAA ATOM 2495 O SER A 338 13.042 8.674 10.594 1.00 41.46 AAAA ATOM 2496 N ILE A 339 10.971 7.898 11.013 1.00 40.11 AAAA ATOM 2497 CA ILE A 339 11.080 7.985 12.461 1.00 39.66 AAAA ATOM 2498 CB ILE A 339 10.061 8.992 13.038 1.00 39.74 AAAA ATOM 2499 CG2 ILE A 339 10.249 9.118 14.544 1.00 38.88 AAAA ATOM 2500 CG1 ILE A 339 10.249 10.354 12.361 1.00 39.75 AAAA ATOM 2501 CD1 ILE A 339 9.263 11.423 12.804 1.00 40.42 AAAA ATOM 2502 C ILE A 339 10.788 6.576 12.978 1.00 40.19 AAAA ATOM 2503 O ILE A 339 9.653 6.102 12.923 1.00 39.97 AAAA ATOM 2504 N PRO A 340 11.821 5.886 13.484 1.00 40.75 AAAA ATOM 2505 CD PRO A 340 13.225 6.336 13.448 1.00 40.95 AAAA ATOM 2506 CA PRO A 340 11.728 4.520 14.012 1.00 40.57 AAAA ATOM 2507 CB PRO A 340 13.161 4.021 13.877 1.00 41.22 AAAA ATOM 2508 CG PRO A 340 13.944 5.244 14.222 1.00 41.12 AAAA ATOM 2509 C PRO A 340 11.180 4.294 15.424 1.00 40.38 AAAA ATOM 2510 O PRO A 340 10.841 3.163 15.776 1.00 40.48 AAAA ATOM 2511 N ASP A 341 11.080 5.345 16.232 1.00 39.43 AAAA ATOM 2512 CA ASP A 341 10.603 5.174 17.603 1.00 38.32 AAAA ATOM 2513 CB ASP A 341 11.668 5.696 18.578 1.00 38.62 AAAA ATOM 2514 CG ASP A 341 12.044 7.146 18.317 1.00 39.54 AAAA ATOM 2515 OD1 ASP A 341 11.727 7.658 17.221 1.00 38.30 AAAA ATOM 2516 OD2 ASP A 341 12.668 7.771 19.209 1.00 40.07 AAAA ATOM 2517 C ASP A 341 9.241 5.789 17.939 1.00 37.27 AAAA ATOM 2518 O ASP A 341 9.014 6.235 19.066 1.00 35.88 AAAA ATOM 2519 N ALA A 342 8.329 5.789 16.971 1.00 36.20 AAAA ATOM 2520 CA ALA A 342 6.996 6.349 17.181 1.00 34.98 AAAA ATOM 2521 CB ALA A 342 6.150 6.156 15.927 1.00 35.84 AAAA ATOM 2522 C ALA A 342 6.280 5.744 18.389 1.00 34.17 AAAA ATOM 2523 O ALA A 342 5.843 6.465 19.289 1.00 33.36 AAAA ATOM 2524 N THR A 343 6.159 4.421 18.410 1.00 33.49 AAAA ATOM 2525 CA THR A 343 5.481 3.747 19.512 1.00 33.39 AAAA ATOM 2526 CB THR A 343 5.567 2.211 19.362 1.00 33.34 AAAA ATOM 2527 OG1 THR A 343 4.951 1.818 18.128 1.00 34.05 AAAA ATOM 2528 CG2 THR A 343 4.851 1.519 20.516 1.00 33.82 AAAA ATOM 2529 C THR A 343 6.067 4.155 20.865 1.00 33.89 AAAA ATOM 2530 O THR A 343 5.340 4.591 21.756 1.00 32.15 AAAA ATOM 2531 N GLU A 344 7.383 4.027 21.007 1.00 34.87 AAAA ATOM 2532 CA GLU A 344 8.055 4.379 22.257 1.00 35.80 AAAA ATOM 2533 CB GLU A 344 9.553 4.054 22.177 1.00 37.79 AAAA ATOM 2534 CG GLU A 344 9.892 2.570 22.029 1.00 41.45 AAAA ATOM 2535 CD GLU A 344 9.963 2.101 20.581 1.00 44.16 AAAA ATOM 2536 OE1 GLU A 344 10.311 0.917 20.357 1.00 45.57 AAAA ATOM 2537 OE2 GLU A 344 9.676 2.910 19.668 1.00 45.28 AAAA ATOM 2538 C GLU A 344 7.886 5.856 22.590 1.00 35.95 AAAA ATOM 2539 O GLU A 344 7.751 6.233 23.754 1.00 35.12 AAAA ATOM 2540 N ARG A 345 7.896 6.689 21.559 1.00 35.83 AAAA ATOM 2541 CA ARG A 345 7.759 8.127 21.731 1.00 36.32 AAAA ATOM 2542 CB ARG A 345 7.999 8.803 20.386 1.00 38.26 AAAA ATOM 2543 CG ARG A 345 8.268 10.280 20.448 1.00 41.85 AAAA ATOM 2544 CD ARG A 345 9.006 10.686 19.194 1.00 44.45 AAAA ATOM 2545 NE ARG A 345 9.194 12.128 19.098 1.00 47.27 AAAA ATOM 2546 CZ ARG A 345 9.855 12.721 18.111 1.00 47.66 AAAA ATOM 2547 NH1 ARG A 345 10.390 11.988 17.144 1.00 48.37 AAAA ATOM 2548 NH2 ARG A 345 9.974 14.042 18.090 1.00 48.27 AAAA ATOM 2549 C ARG A 345 6.384 8.510 22.289 1.00 35.99 AAAA ATOM 2550 O ARG A 345 6.285 9.209 23.302 1.00 35.24 AAAA ATOM 2551 N VAL A 346 5.324 8.052 21.630 1.00 34.14 AAAA ATOM 2552 CA VAL A 346 3.975 8.355 22.092 1.00 33.40 AAAA ATOM 2553 CB VAL A 346 2.909 7.816 21.110 1.00 33.26 AAAA ATOM 2554 CG1 VAL A 346 1.516 7.969 21.709 1.00 33.83 AAAA ATOM 2555 CG2 VAL A 346 3.005 8.565 19.793 1.00 32.47 AAAA ATOM 2556 C VAL A 346 3.770 7.727 23.466 1.00 33.14 AAAA ATOM 2557 O VAL A 346 3.172 8.336 24.352 1.00 32.24 AAAA ATOM 2558 N ALA A 347 4.280 6.510 23.643 1.00 32.01 AAAA ATOM 2559 CA ALA A 347 4.159 5.813 24.917 1.00 32.80 AAAA ATOM 2560 CB ALA A 347 4.831 4.447 24.839 1.00 31.97 AAAA ATOM 2561 C ALA A 347 4.788 6.639 26.031 1.00 33.01 AAAA ATOM 2562 O ALA A 347 4.214 6.769 27.114 1.00 32.22 AAAA ATOM 2563 N ASN A 348 5.968 7.193 25.758 1.00 33.65 AAAA ATOM 2564 CA ASN A 348 6.681 8.009 26.738 1.00 35.77 AAAA ATOM 2565 CB ASN A 348 8.078 8.382 26.228 1.00 37.45 AAAA ATOM 2566 CG ASN A 348 8.996 7.183 26.119 1.00 40.90 AAAA ATOM 2567 OD1 ASN A 348 8.998 6.308 26.989 1.00 43.23 AAAA ATOM 2568 ND2 ASN A 348 9.795 7.140 25.057 1.00 42.50 AAAA ATOM 2569 C ASN A 348 5.912 9.281 27.074 1.00 35.43 AAAA ATOM 2570 O ASN A 348 5.824 9.662 28.240 1.00 34.83 AAAA ATOM 2571 N GLU A 349 5.372 9.943 26.051 1.00 35.34 AAAA ATOM 2572 CA GLU A 349 4.600 11.164 26.264 1.00 34.80 AAAA ATOM 2573 CB GLU A 349 4.203 11.802 24.932 1.00 36.04 AAAA ATOM 2574 CG GLU A 349 5.277 12.681 24.323 1.00 38.86 AAAA ATOM 2575 CD GLU A 349 5.713 13.801 25.257 1.00 40.72 AAAA ATOM 2576 OE1 GLU A 349 4.836 14.458 25.860 1.00 41.85 AAAA ATOM 2577 OE2 GLU A 349 6.933 14.033 25.385 1.00 42.23 AAAA ATOM 2578 C GLU A 349 3.357 10.863 27.084 1.00 32.75 AAAA ATOM 2579 O GLU A 349 2.962 11.658 27.932 1.00 32.53 AAAA ATOM 2580 N VAL A 350 2.737 9.716 26.827 1.00 31.83 AAAA ATOM 2581 CA VAL A 350 1.556 9.323 27.583 1.00 31.06 AAAA ATOM 2582 CB VAL A 350 0.952 8.000 27.049 1.00 31.68 AAAA ATOM 2583 CG1 VAL A 350 0.006 7.406 28.081 1.00 31.12 AAAA ATOM 2584 CG2 VAL A 350 0.205 8.260 25.753 1.00 31.66 AAAA ATOM 2585 C VAL A 350 1.949 9.135 29.048 1.00 30.82 AAAA ATOM 2586 O VAL A 350 1.239 9.579 29.953 1.00 30.31 AAAA ATOM 2587 N SER A 351 3.087 8.486 29.276 1.00 29.94 AAAA ATOM 2588 CA SER A 351 3.569 8.248 30.635 1.00 31.15 AAAA ATOM 2589 CB SER A 351 4.830 7.378 30.610 1.00 31.12 AAAA ATOM 2590 OG SER A 351 5.292 7.138 31.926 1.00 32.12 AAAA ATOM 2591 C SER A 351 3.880 9.558 31.351 1.00 30.90 AAAA ATOM 2592 O SER A 351 3.556 9.731 32.527 1.00 30.97 AAAA ATOM 2593 N ARG A 352 4.511 10.478 30.633 1.00 31.65 AAAA ATOM 2594 CA ARG A 352 4.873 11.771 31.193 1.00 33.50 AAAA ATOM 2595 CB ARG A 352 5.681 12.572 30.172 1.00 35.69 AAAA ATOM 2596 CG ARG A 352 6.406 13.776 30.753 1.00 40.36 AAAA ATOM 2597 CD ARG A 352 6.877 14.713 29.652 1.00 43.61 AAAA ATOM 2598 NE ARG A 352 5.742 15.305 28.947 1.00 47.26 AAAA ATOM 2599 CZ ARG A 352 5.846 16.181 27.952 1.00 49.17 AAAA ATOM 2600 NH1 ARG A 352 7.043 16.575 27.532 1.00 50.34 AAAA ATOM 2601 NH2 ARG A 352 4.751 16.670 27.381 1.00 49.80 AAAA ATOM 2602 C ARG A 352 3.623 12.558 31.588 1.00 33.09 AAAA ATOM 2603 O ARG A 352 3.570 13.159 32.660 1.00 33.61 AAAA ATOM 2604 N VAL A 353 2.622 12.554 30.713 1.00 32.09 AAAA ATOM 2605 CA VAL A 353 1.380 13.272 30.975 1.00 32.29 AAAA ATOM 2606 CB VAL A 353 0.490 13.307 29.714 1.00 31.98 AAAA ATOM 2607 CG1 VAL A 353 −0.897 13.828 30.062 1.00 30.21 AAAA ATOM 2608 CG2 VAL A 353 1.129 14.200 28.665 1.00 30.41 AAAA ATOM 2609 C VAL A 353 0.596 12.660 32.131 1.00 32.54 AAAA ATOM 2610 O VAL A 353 0.075 13.379 32.985 1.00 32.79 AAAA ATOM 2611 N ALA A 354 0.513 11.335 32.159 1.00 32.97 AAAA ATOM 2612 CA ALA A 354 −0.206 10.650 33.224 1.00 34.65 AAAA ATOM 2613 CB ALA A 354 −0.157 9.145 33.007 1.00 33.53 AAAA ATOM 2614 C ALA A 354 0.391 11.002 34.583 1.00 35.84 AAAA ATOM 2615 O ALA A 354 −0.316 11.026 35.588 1.00 36.31 AAAA ATOM 2616 N ARG A 355 1.694 11.271 34.609 1.00 38.21 AAAA ATOM 2617 CA ARG A 355 2.382 11.619 35.852 1.00 41.12 AAAA ATOM 2618 CB ARG A 355 3.637 11.141 35.802 1.00 42.43 AAAA ATOM 2619 CG ARG A 355 3.976 9.627 35.701 1.00 44.93 AAAA ATOM 2620 CD ARG A 355 5.416 9.190 35.457 1.00 47.18 AAAA ATOM 2621 NE ARG A 355 5.482 7.790 35.042 1.00 48.82 AAAA ATOM 2622 CZ ARG A 355 5.248 6.754 35.842 1.00 50.06 AAAA ATOM 2623 NH1 ARG A 355 4.939 6.947 37.117 1.00 50.68 AAAA ATOM 2624 NH2 ARG A 355 5.302 5.519 35.360 1.00 50.06 AAAA ATOM 2625 C ARG A 355 2.333 13.125 36.103 1.00 42.42 AAAA ATOM 2626 O ARG A 355 2.883 13.621 37.086 1.00 42.30 AAAA ATOM 2627 N ALA A 356 1.660 13.840 35.203 1.00 43.60 AAAA ATOM 2628 CA ALA A 356 1.504 15.289 35.294 1.00 44.67 AAAA ATOM 2629 CB ALA A 356 0.702 15.651 36.547 1.00 45.12 AAAA ATOM 2630 C ALA A 356 2.830 16.042 35.288 1.00 45.36 AAAA ATOM 2631 O ALA A 356 2.980 17.042 35.989 1.00 45.40 AAAA ATOM 2632 N LEU A 357 3.779 15.569 34.487 1.00 46.31 AAAA ATOM 2633 CA LEU A 357 5.093 16.201 34.392 1.00 47.87 AAAA ATOM 2634 CB LEU A 357 6.122 15.212 33.843 1.00 47.62 AAAA ATOM 2635 CG LEU A 357 6.465 14.017 34.734 1.00 47.58 AAAA ATOM 2636 CD1 LEU A 357 7.330 13.041 33.958 1.00 47.32 AAAA ATOM 2637 CD2 LEU A 357 7.187 14.497 35.985 1.00 47.50 AAAA ATOM 2638 C LEU A 357 5.064 17.438 33.505 1.00 48.87 AAAA ATOM 2639 OT1 LEU A 357 5.458 18.518 33.993 1.00 50.17 AAAA ATOM 2640 OT2 LEU A 357 4.659 17.313 32.330 1.00 50.17 AAAA ATOM 2641 CB LYS B 7 −5.082 −44.913 −47.742 1.00 46.68 BBBB ATOM 2642 CG LYS B 7 −4.666 −44.949 −49.196 1.00 49.02 BBBB ATOM 2643 CD LYS B 7 −3.162 −44.896 −49.340 1.00 49.96 BBBB ATOM 2644 CE LYS B 7 −2.769 −45.054 −50.794 1.00 50.91 BBBB ATOM 2645 NZ LYS B 7 −1.300 −45.222 −50.954 1.00 52.39 BBBB ATOM 2646 C LYS B 7 −6.742 −45.658 −46.035 1.00 43.87 BBBB ATOM 2647 O LYS B 7 −7.135 −44.760 −45.287 1.00 43.90 BBBB ATOM 2648 N LYS B 7 −7.490 −44.434 −48.090 1.00 46.26 BBBB ATOM 2649 CA LYS B 7 −6.512 −45.403 −47.519 1.00 45.28 BBBB ATOM 2650 N ARG B 8 −6.486 −46.895 −45.620 1.00 41.24 BBBB ATOM 2651 CA ARG B 8 −6.682 −47.303 −44.240 1.00 38.63 BBBB ATOM 2652 CB ARG B 8 −7.493 −48.600 −44.201 1.00 40.59 BBBB ATOM 2653 CG ARG B 8 −8.927 −48.466 −44.677 1.00 43.69 BBBB ATOM 2654 CD ARG B 8 −9.417 −49.774 −45.269 1.00 46.42 BBBB ATOM 2655 NE ARG B 8 −10.866 −49.789 −45.425 1.00 50.16 BBBB ATOM 2656 CZ ARG B 8 −11.722 −49.833 −44.408 1.00 51.89 BBBB ATOM 2657 NH1 ARG B 8 −11.268 −49.869 −43.165 1.00 52.20 BBBB ATOM 2658 NH2 ARG B 8 −13.031 −49.841 −44.631 1.00 53.20 BBBB ATOM 2659 C ARG B 8 −5.371 −47.512 −43.495 1.00 35.87 BBBB ATOM 2660 O ARG B 8 −4.474 −48.206 −43.973 1.00 34.76 BBBB ATOM 2661 N LEU B 9 −5.272 −46.899 −42.321 1.00 32.91 BBBB ATOM 2662 CA LEU B 9 −4.094 −47.039 −41.477 1.00 30.88 BBBB ATOM 2663 CB LEU B 9 −3.390 −45.694 −41.278 1.00 30.40 BBBB ATOM 2664 CG LEU B 9 −2.381 −45.626 −40.119 1.00 29.02 BBBB ATOM 2665 CD1 LEU B 9 −1.157 −46.466 −40.442 1.00 29.47 BBBB ATOM 2666 CD2 LEU B 9 −1.975 −44.178 −39.873 1.00 29.56 BBBB ATOM 2667 C LEU B 9 −4.513 −47.562 −40.115 1.00 29.67 BBBB ATOM 2668 O LEU B 9 −5.505 −47.101 −39.543 1.00 28.43 BBBB ATOM 2669 N MET B 10 −3.772 −48.541 −39.604 1.00 27.75 BBBB ATOM 2670 CA MET B 10 −4.048 −49.055 −38.275 1.00 26.66 BBBB ATOM 2671 CB MET B 10 −4.268 −50.571 −38.274 1.00 27.09 BBBB ATOM 2672 CG MET B 10 −4.496 −51.113 −36.869 1.00 28.55 BBBB ATOM 2673 SD MET B 10 −5.474 −52.612 −36.799 1.00 29.60 BBBB ATOM 2674 CE MET B 10 −7.126 −51.913 −36.618 1.00 29.41 BBBB ATOM 2675 C MET B 10 −2.826 −48.691 −37.448 1.00 25.08 BBBB ATOM 2676 O MET B 10 −1.690 −48.971 −37.839 1.00 24.38 BBBB ATOM 2677 N VAL B 11 −3.062 −48.037 −36.317 1.00 23.45 BBBB ATOM 2678 CA VAL B 11 −1.982 −47.605 −35.449 1.00 23.16 BBBB ATOM 2679 CB VAL B 11 −2.159 −46.116 −35.029 1.00 23.01 BBBB ATOM 2680 CG1 VAL B 11 −0.971 −45.666 −34.184 1.00 20.91 BBBB ATOM 2681 CG2 VAL B 11 −2.305 −45.225 −36.276 1.00 23.82 BBBB ATOM 2682 C VAL B 11 −1.935 −48.461 −34.184 1.00 23.59 BBBB ATOM 2683 O VAL B 11 −2.962 −48.712 −33.567 1.00 23.24 BBBB ATOM 2684 N MET B 12 −0.734 −48.902 −33.817 1.00 23.68 BBBB ATOM 2685 CA MET B 12 −0.523 −49.707 −32.613 1.00 24.54 BBBB ATOM 2686 CB MET B 12 0.192 −51.019 −32.971 1.00 24.28 BBBB ATOM 2687 CG MET B 12 −0.402 −51.726 −34.188 1.00 25.19 BBBB ATOM 2688 SD MET B 12 0.399 −53.284 −34.669 1.00 26.54 BBBB ATOM 2689 CE MET B 12 1.990 −52.691 −35.289 1.00 22.99 BBBB ATOM 2690 C MET B 12 0.361 −48.840 −31.720 1.00 25.31 BBBB ATOM 2691 O MET B 12 1.546 −48.645 −32.006 1.00 23.88 BBBB ATOM 2692 N ALA B 13 −0.224 −48.292 −30.657 1.00 27.08 BBBB ATOM 2693 CA ALA B 13 0.508 −47.410 −29.752 1.00 29.43 BBBB ATOM 2694 CB ALA B 13 0.747 −46.074 −30.429 1.00 28.82 BBBB ATOM 2695 C ALA B 13 −0.239 −47.192 −28.436 1.00 31.80 BBBB ATOM 2696 O ALA B 13 −1.143 −46.350 −28.352 1.00 32.16 BBBB ATOM 2697 N GLY B 14 0.150 −47.934 −27.405 1.00 32.46 BBBB ATOM 2698 CA GLY B 14 −0.513 −47.804 −26.120 1.00 33.82 BBBB ATOM 2699 C GLY B 14 −0.107 −46.595 −25.299 1.00 34.82 BBBB ATOM 2700 O GLY B 14 0.975 −46.040 −25.479 1.00 35.47 BBBB ATOM 2701 N GLY B 15 −0.986 −46.188 −24.385 1.00 35.56 BBBB ATOM 2702 CA GLY B 15 −0.700 −45.047 −23.536 1.00 36.08 BBBB ATOM 2703 C GLY B 15 0.539 −45.254 −22.683 1.00 36.84 BBBB ATOM 2704 O GLY B 15 1.293 −44.311 −22.426 1.00 36.03 BBBB ATOM 2705 N THR B 16 0.755 −46.488 −22.240 1.00 36.65 BBBB ATOM 2706 CA THR B 16 1.920 −46.787 −21.421 1.00 38.51 BBBB ATOM 2707 CB THR B 16 1.926 −48.258 − 20.974 1.00 38.51 BBBB ATOM 2708 OG1 THR B 16 0.686 −48.558 −20.321 1.00 38.39 BBBB ATOM 2709 CG2 THR B 16 3.075 −48.518 −20.005 1.00 39.11 BBBB ATOM 2710 C THR B 16 3.158 −46.497 −22.264 1.00 38.35 BBBB ATOM 2711 O THR B 16 3.191 −46.798 −23.460 1.00 39.90 BBBB ATOM 2712 N GLY B 17 4.168 −45.897 −21.649 1.00 37.68 BBBB ATOM 2713 CA GLY B 17 5.367 −45.567 −22.392 1.00 36.57 BBBB ATOM 2714 C GLY B 17 5.161 −44.303 −23.211 1.00 35.56 BBBB ATOM 2715 O GLY B 17 6.079 −43.843 −23.890 1.00 35.03 BBBB ATOM 2716 N GLY B 18 3.949 −43.752 −23.150 1.00 33.83 BBBB ATOM 2717 CA GLY B 18 3.631 −42.529 −23.872 1.00 33.48 BBBB ATOM 2718 C GLY B 18 3.825 −42.593 −25.378 1.00 33.12 BBBB ATOM 2719 O GLY B 18 4.345 −41.650 −25.984 1.00 35.38 BBBB ATOM 2720 N HIS B 19 3.416 −43.699 −25.988 1.00 30.26 BBBB ATOM 2721 CA HIS B 19 3.548 −43.865 −27.435 1.00 28.22 BBBB ATOM 2722 CB HIS B 19 3.772 −45.349 −27.779 1.00 25.81 BBBB ATOM 2723 CG HIS B 19 4.957 −45.966 −27.094 1.00 25.35 BBBB ATOM 2724 CD2 HIS B 19 6.281 −45.694 −27.184 1.00 24.18 BBBB ATOM 2725 ND1 HIS B 19 4.845 −47.025 −26.217 1.00 24.57 BBBB ATOM 2726 CE1 HIS B 19 6.046 −47.380 −25.798 1.00 23.08 BBBB ATOM 2727 NE2 HIS B 19 6.936 −46.589 −26.369 1.00 25.51 BBBB ATOM 2728 C HIS B 19 2.280 −43.370 −28.144 1.00 27.91 BBBB ATOM 2729 O HIS B 19 2.300 −43.049 −29.337 1.00 26.91 BBBB ATOM 2730 N VAL B 20 1.180 −43.310 −27.402 1.00 27.65 BBBB ATOM 2731 CA VAL B 20 −0.098 −42.894 −27.965 1.00 27.77 BBBB ATOM 2732 CB VAL B 20 −1.248 −43.080 −26.942 1.00 28.57 BBBB ATOM 2733 CG1 VAL B 20 −1.082 −42.114 −25.787 1.00 30.03 BBBB ATOM 2734 CG2 VAL B 20 −2.602 −42.873 −27.631 1.00 26.82 BBBB ATOM 2735 C VAL B 20 −0.140 −41.452 −28.470 1.00 27.57 BBBB ATOM 2736 O VAL B 20 −0.771 −41.172 −29.486 1.00 27.12 BBBB ATOM 2737 N PHE B 21 0.528 −40.543 −27.770 1.00 28.03 BBBB ATOM 2738 CA PHE B 21 0.517 −39.136 −28.160 1.00 29.00 BBBB ATOM 2739 CB PHE B 21 1.215 −38.289 −27.094 1.00 30.27 BBBB ATOM 2740 CG PHE B 21 0.565 −38.383 −25.746 1.00 33.59 BBBB ATOM 2741 CD1 PHE B 21 − 0.764 −37.999 −25.578 1.00 33.84 BBBB ATOM 2742 CD2 PHE B 21 1.256 −38.909 −24.659 1.00 35.22 BBBB ATOM 2743 CE1 PHE B 21 −1.397 −38.142 −24.350 1.00 35.17 BBBB ATOM 2744 CE2 PHE B 21 0.630 −39.057 −23.422 1.00 36.08 BBBB ATOM 2745 CZ PHE B 21 −0.700 −38.673 −23.269 1.00 35.65 BBBB ATOM 2746 C PHE B 21 1.129 −38.898 −29.535 1.00 28.53 BBBB ATOM 2747 O PHE B 21 0.521 −38.236 −30.378 1.00 28.69 BBBB ATOM 2748 N PRO B 22 2.336 −39.430 −29.781 1.00 27.41 BBBB ATOM 2749 CD PRO B 22 3.251 −40.074 −28.819 1.00 27.82 BBBB ATOM 2750 CA PRO B 22 2.986 −39.252 −31.086 1.00 26.12 BBBB ATOM 2751 CB PRO B 22 4.362 −39.884 −30.883 1.00 27.48 BBBB ATOM 2752 CG PRO B 22 4.594 −39.757 −29.403 1.00 28.99 BBBB ATOM 2753 C PRO B 22 2.188 −39.972 −32.176 1.00 26.37 BBBB ATOM 2754 O PRO B 22 2.129 −39.522 −33.321 1.00 24.40 BBBB ATOM 2755 N GLY B 23 1.585 −41.102 −31.807 1.00 24.71 BBBB ATOM 2756 CA GLY B 23 0.787 −41.864 −32.752 1.00 25.07 BBBB ATOM 2757 C GLY B 23 −0.459 −41.088 −33.144 1.00 25.00 BBBB ATOM 2758 O GLY B 23 −0.913 −41.144 −34.295 1.00 23.40 BBBB ATOM 2759 N LEU B 24 −1.014 −40.366 −32.176 1.00 24.65 BBBB ATOM 2760 CA LEU B 24 −2.201 −39.551 −32.401 1.00 25.32 BBBB ATOM 2761 CB LEU B 24 −2.732 −39.017 −31.064 1.00 25.08 BBBB ATOM 2762 CG LEU B 24 −3.594 −39.997 −30.264 1.00 23.58 BBBB ATOM 2763 CD1 LEU B 24 −3.823 −39.482 −28.828 1.00 25.41 BBBB ATOM 2764 CD2 LEU B 24 −4.919 −40.192 −30.998 1.00 24.78 BBBB ATOM 2765 C LEU B 24 −1.843 −38.397 −33.336 1.00 25.69 BBBB ATOM 2766 O LEU B 24 −2.634 −38.017 −34.204 1.00 25.99 BBBB ATOM 2767 N ALA B 25 −0.644 −37.850 −33.164 1.00 24.89 BBBB ATOM 2768 CA ALA B 25 −0.197 −36.754 −34.013 1.00 25.94 BBBB ATOM 2769 CB ALA B 25 1.195 −36.278 −33.590 1.00 25.12 BBBB ATOM 2770 C ALA B 25 −0.171 −37.207 −35.469 1.00 27.14 BBBB ATOM 2771 O ALA B 25 −0.626 −36.483 −36.354 1.00 27.46 BBBB ATOM 2772 N VAL B 26 0.368 −38.403 −35.709 1.00 26.50 BBBB ATOM 2773 CA VAL B 26 0.466 −38.955 −37.056 1.00 25.70 BBBB ATOM 2774 CB VAL B 26 1.373 −40.226 −37.081 1.00 26.22 BBBB ATOM 2775 CG1 VAL B 26 1.410 −40.833 −38.479 1.00 26.25 BBBB ATOM 2776 CG2 VAL B 26 2.778 −39.861 −36.631 1.00 24.56 BBBB ATOM 2777 C VAL B 26 −0.908 −39.310 −37.612 1.00 26.20 BBBB ATOM 2778 O VAL B 26 −1.178 −39.091 −38.796 1.00 25.87 BBBB ATOM 2779 N ALA B 27 −1.777 −39.851 −36.764 1.00 24.68 BBBB ATOM 2780 CA ALA B 27 −3.116 −40.222 −37.199 1.00 26.15 BBBB ATOM 2781 CB ALA B 27 −3.868 −40.909 −36.066 1.00 26.23 BBBB ATOM 2782 C ALA B 27 −3.888 −38.984 −37.661 1.00 27.60 BBBB ATOM 2783 O ALA B 27 −4.492 −38.985 −38.736 1.00 27.05 BBBB ATOM 2784 N HIS B 28 −3.864 −37.933 −36.847 1.00 27.68 BBBB ATOM 2785 CA HIS B 28 −4.574 −36.702 −37.190 1.00 29.32 BBBB ATOM 2786 CB HIS B 28 −4.498 −35.693 −36.039 1.00 27.05 BBBB ATOM 2787 CG HIS B 28 −5.491 −35.957 −34.952 1.00 27.65 BBBB ATOM 2788 CD2 HIS B 28 −5.327 −36.213 −33.632 1.00 26.92 BBBB ATOM 2789 ND1 HIS B 28 −6.850 −36.010 −35.188 1.00 27.29 BBBB ATOM 2790 CE1 HIS B 28 −7.479 −36.290 −34.060 1.00 26.85 BBBB ATOM 2791 NE2 HIS B 28 −6.578 −36.417 −33.101 1.00 27.78 BBBB ATOM 2792 C HIS B 28 −4.018 −36.095 −38.462 1.00 30.24 BBBB ATOM 2793 O HIS B 28 −4.766 −35.589 −39.297 1.00 31.14 BBBB ATOM 2794 N HIS B 29 −2.702 −36.164 −38.618 1.00 31.42 BBBB ATOM 2795 CA HIS B 29 −2.070 −35.623 −39.806 1.00 32.38 BBBB ATOM 2796 CB HIS B 29 −0.554 −35.764 −39.720 1.00 33.49 BBBB ATOM 2797 CG HIS B 29 0.177 −34.957 −40.743 1.00 35.61 BBBB ATOM 2798 CD2 HIS B 29 0.667 −35.292 −41.960 1.00 36.38 BBBB ATOM 2799 ND1 HIS B 29 0.436 −33.612 −40.583 1.00 37.53 BBBB ATOM 2800 CE1 HIS B 29 1.055 −33.155 −41.657 1.00 37.93 BBBB ATOM 2801 NE2 HIS B 29 1.207 −34.154 −42.508 1.00 37.24 BBBB ATOM 2802 C HIS B 29 −2.567 −36.324 −41.068 1.00 33.00 BBBB ATOM 2803 O HIS B 29 −2.845 −35.674 −42.078 1.00 33.02 BBBB ATOM 2804 N LEU B 30 −2.676 −37.650 −41.012 1.00 31.69 BBBB ATOM 2805 CA LEU B 30 −3.136 −38.417 −42.162 1.00 32.00 BBBB ATOM 2806 CB LEU B 30 −2.701 −39.883 −42.033 1.00 30.44 BBBB ATOM 2807 CG LEU B 30 − 1.191 −40.099 −42.203 1.00 29.95 BBBB ATOM 2808 CD1 LEU B 30 −0.823 −41.550 −41.898 1.00 28.64 BBBB ATOM 2809 CD2 LEU B 30 −0.785 −39.736 −43.621 1.00 28.97 BBBB ATOM 2810 C LEU B 30 −4.641 −38.332 −42.375 1.00 32.37 BBBB ATOM 2811 O LEU B 30 −5.109 −38.414 −43.507 1.00 33.16 BBBB ATOM 2812 N MET B 31 −5.401 −38.168 −41.297 1.00 33.50 BBBB ATOM 2813 CA MET B 31 − 6.849 −38.064 −41.424 1.00 34.91 BBBB ATOM 2814 CB MET B 31 − 7.514 −38.061 −40.048 1.00 35.67 BBBB ATOM 2815 CG MET B 31 − 7.536 −39.424 −39.391 1.00 36.44 BBBB ATOM 2816 SD MET B 31 − 8.407 −39.436 −37.827 1.00 37.84 BBBB ATOM 2817 CE MET B 31 − 7.095 −39.039 −36.719 1.00 37.80 BBBB ATOM 2818 C MET B 31 −7.197 −36.786 −42.173 1.00 35.99 BBBB ATOM 2819 O MET B 31 −8.224 −36.710 −42.847 1.00 37.36 BBBB ATOM 2820 N ALA B 32 −6.326 −35.791 −42.052 1.00 36.39 BBBB ATOM 2821 CA ALA B 32 − 6.510 −34.511 −42.722 1.00 37.55 BBBB ATOM 2822 CB ALA B 32 − 5.622 −33.458 −42.073 1.00 36.85 BBBB ATOM 2823 C ALA B 32 −6.151 −34.663 −44.205 1.00 38.60 BBBB ATOM 2824 O ALA B 32 −6.392 −33.760 −45.013 1.00 38.04 BBBB ATOM 2825 N GLN B 33 −5.569 −35.809 −44.555 1.00 38.35 BBBB ATOM 2826 CA GLN B 33 − 5.182 −36.070 −45.938 1.00 38.24 BBBB ATOM 2827 CB GLN B 33 − 3.792 −36.706 −46.011 1.00 39.81 BBBB ATOM 2828 CG GLN B 33 − 2.771 −36.162 −45.028 1.00 41.67 BBBB ATOM 2829 CD GLN B 33 − 2.269 −34.781 −45.384 1.00 41.96 BBBB ATOM 2830 OE1 GLN B 33 − 1.735 −34.559 −46.471 1.00 41.35 BBBB ATOM 2831 NE2 GLN B 33 −2.423 −33.843 −44.456 1.00 42.42 BBBB ATOM 2832 C GLN B 33 −6.187 −37.027 −46.556 1.00 36.70 BBBB ATOM 2833 O GLN B 33 − 5.970 −37.541 −47.647 1.00 36.47 BBBB ATOM 2834 N GLY B 34 −7.281 −37.274 −45.845 1.00 36.09 BBBB ATOM 2835 CA GLY B 34 − 8.305 −38.169 −46.353 1.00 35.75 BBBB ATOM 2836 C GLY B 34 −8.219 −39.600 −45.837 1.00 35.33 BBBB ATOM 2837 O GLY B 34 −9.075 −40.426 −46.146 1.00 34.43 BBBB ATOM 2838 N TRP B 35 − 7.196 −39.896 −45.042 1.00 35.23 BBBB ATOM 2839 CA TRP B 35 − 7.016 −41.246 −44.508 1.00 34.58 BBBB ATOM 2840 CB TRP B 35 −5.618 −41.400 −43.908 1.00 35.03 BBBB ATOM 2841 CG TRP B 35 −4.511 −41.558 −44.901 1.00 34.87 BBBB ATOM 2842 CD2 TRP B 35 − 3.666 −42.704 −45.060 1.00 35.81 BBBB ATOM 2843 CE2 TRP B 35 − 2.733 −42.399 −46.076 1.00 35.60 BBBB ATOM 2844 CE3 TRP B 35 −3.605 −43.961 −44.441 1.00 36.59 BBBB ATOM 2845 CD1 TRP B 35 −4.075 −40.633 −45.803 1.00 35.62 BBBB ATOM 2846 NE1 TRP B 35 −3.004 −41.129 −46.513 1.00 34.95 BBBB ATOM 2847 CZ2 TRP B 35 −1.746 −43.305 −46.488 1.00 37.19 BBBB ATOM 2848 CZ3 TRP B 35 −2.620 −44.865 −44.852 1.00 36.85 BBBB ATOM 2849 CH2 TRP B 35 −1.705 −44.528 −45.867 1.00 36.87 BBBB ATOM 2850 C TRP B 35 −8.022 −41.670 −43.449 1.00 34.58 BBBB ATOM 2851 O TRP B 35 −8.546 −40.850 −42.699 1.00 33.58 BBBB ATOM 2852 N GLN B 36 −8.295 −42.969 −43.410 1.00 34.54 BBBB ATOM 2853 CA GLN B 36 − 9.175 −43.535 −42.402 1.00 35.40 BBBB ATOM 2854 CB GLN B 36 −10.095 −44.596 −43.003 1.00 37.42 BBBB ATOM 2855 CG GLN B 36 − 11.219 −44.027 −43.862 1.00 41.66 BBBB ATOM 2856 CD GLN B 36 −11.996 −45.103 −44.601 1.00 44.12 BBBB ATOM 2857 OE1 GLN B 36 −12.988 −44.816 −45.277 1.00 45.76 BBBB ATOM 2858 NE2 GLN B 36 − 11.546 −46.350 −44.480 1.00 44.99 BBBB ATOM 2859 C GLN B 36 −8.183 −44.186 −41.451 1.00 34.89 BBBB ATOM 2860 O GLN B 36 −7.272 −44.885 −41.889 1.00 34.58 BBBB ATOM 2861 N VAL B 37 −8.336 −43.941 −40.158 1.00 35.26 BBBB ATOM 2862 CA VAL B 37 −7.417 −44.516 −39.184 1.00 34.16 BBBB ATOM 2863 CB VAL B 37 −6.561 −43.417 −38.509 1.00 34.99 BBBB ATOM 2864 GC1 VAL B 37 −5.630 −44.032 −37.479 1.00 34.72 BBBB ATOM 2865 CG2 VAL B 37 −5.755 −42.668 −39.552 1.00 34.06 BBBB ATOM 2866 C VAL B 37 −8.166 −45.288 −38.109 1.00 34.02 BBBB ATOM 2867 O VAL B 37 −9.207 −44.849 −37.618 1.00 33.01 BBBB ATOM 2868 N ARG B 38 −7.629 −46.451 −37.758 1.00 32.20 BBBB ATOM 2869 CA ARG B 38 − 8.219 −47.286 −36.730 1.00 31.56 BBBB ATOM 2870 CB ARG B 38 −8.811 −48.554 −37.344 1.00 33.53 BBBB ATOM 2871 CG ARG B 38 −9.706 −49.324 −36.397 1.00 36.77 BBBB ATOM 2872 CD ARG B 38 −11.107 −49.511 −36.975 1.00 38.80 BBBB ATOM 2873 NE ARG B 38 − 12.000 −50.108 −35.989 1.00 41.24 BBBB ATOM 2874 CZ ARG B 38 −13.304 −50.293 −36.161 1.00 43.18 BBBB ATOM 2875 NH1 ARG B 38 −13.892 −49.927 −37.294 1.00 43.21 BBBB ATOM 2876 NH2 ARG B 38 −14.026 −50.839 −35.189 1.00 44.37 BBBB ATOM 2877 C ARG B 38 −7.097 −47.628 −35.751 1.00 30.48 BBBB ATOM 2878 O ARG B 38 −5.936 −47.742 −36.134 1.00 29.62 BBBB ATOM 2879 N TRP B 39 −7.447 −47.782 −34.484 1.00 28.40 BBBB ATOM 2880 CA TRP B 39 −6.456 −48.070 −33.471 1.00 27.41 BBBB ATOM 2881 CB TRP B 39 −6.696 −47.145 −32.291 1.00 27.98 BBBB ATOM 2882 CG TRP B 39 −5.480 −46.788 −31.568 1.00 28.00 BBBB ATOM 2883 CD2 TRP B 39 −4.677 −45.627 −31.784 1.00 28.42 BBBB ATOM 2884 CE2 TRP B 39 −3.625 −45.673 −30.851 1.00 28.85 BBBB ATOM 2885 CE3 TRP B 39 −4.749 −44.549 −32.680 1.00 29.78 BBBB ATOM 2886 CD1 TRP B 39 −4.898 −47.476 −30.549 1.00 28.26 BBBB ATOM 2887 NE1 TRP B 39 −3.783 −46.812 −30.111 1.00 28.48 BBBB ATOM 2888 CZ2 TRP B 39 −2.648 −44.684 −30.778 1.00 30.55 BBBB ATOM 2889 CZ3 TRP B 39 −3.770 −43.561 −32.610 1.00 29.22 BBBB ATOM 2890 CH2 TRP B 39 −2.734 −43.639 −31.662 1.00 30.90 BBBB ATOM 2891 C TRP B 39 −6.478 −49.517 −32.999 1.00 25.82 BBBB ATOM 2892 O TRP B 39 −7.509 −50.176 −33.055 1.00 24.87 BBBB ATOM 2893 N LEU B 40 −5.323 −50.004 −32.549 1.00 25.21 BBBB ATOM 2894 CA LEU B 40 −5.200 −51.364 −32.026 1.00 24.71 BBBB ATOM 2895 CB LEU B 40 −4.326 −52.221 −32.952 1.00 25.21 BBBB ATOM 2896 CG LEU B 40 −4.416 −53.754 −32.868 1.00 26.95 BBBB ATOM 2897 CD1 LEU B 40 −3.037 −54.334 −32.571 1.00 27.63 BBBB ATOM 2898 CD2 LEU B 40 −5.421 −54.179 −31.817 1.00 26.69 BBBB ATOM 2899 C LEU B 40 −4.535 −51.235 −30.655 1.00 23.33 BBBB ATOM 2900 O LEU B 40 −3.387 −50.824 −30.563 1.00 23.43 BBBB ATOM 2901 N GLY B 41 −5.260 −51.567 −29.591 1.00 24.01 BBBB ATOM 2902 CA GLY B 41 −4.691 −51.450 −28.257 1.00 23.47 BBBB ATOM 2903 C GLY B 41 −5.292 −52.479 −27.322 1.00 23.99 BBBB ATOM 2904 O GLY B 41 −5.797 −53.498 −27.785 1.00 22.90 BBBB ATOM 2905 N THR B 42 −5.225 −52.225 −26.017 1.00 26.62 BBBB ATOM 2906 CA THR B 42 −5.787 −53.141 −25.027 1.00 29.84 BBBB ATOM 2907 CB THR B 42 −4.693 −53.715 −24.092 1.00 30.17 BBBB ATOM 2908 OG1 THR B 42 −4.019 −52.647 −23.418 1.00 30.77 BBBB ATOM 2909 CG2 THR B 42 −3.683 −54.514 −24.900 1.00 31.30 BBBB ATOM 2910 C THR B 42 −6.852 −52.420 −24.200 1.00 32.04 BBBB ATOM 2911 O THR B 42 −6.737 −51.226 −23.924 1.00 31.27 BBBB ATOM 2912 N ALA B 43 −7.881 −53.160 −23.801 1.00 35.37 BBBB ATOM 2913 CA ALA B 43 −9.000 −52.595 −23.047 1.00 38.81 BBBB ATOM 2914 CB ALA B 43 −10.063 −53.669 −22.835 1.00 38.49 BBBB ATOM 2915 C ALA B 43 −8.671 −51.928 −21.713 1.00 41.06 BBBB ATOM 2916 O ALA B 43 −9.224 −50.875 −21.391 1.00 42.22 BBBB ATOM 2917 N ASP B 44 −7.777 −52.521 − 20.931 1.00 43.18 BBBB ATOM 2918 CA ASP B 44 −7.455 −51.942 − 19.632 1.00 44.47 BBBB ATOM 2919 CB ASP B 44 −7.311 −53.057 − 18.586 1.00 46.93 BBBB ATOM 2920 CG ASP B 44 −8.646 −53.724 − 18.255 1.00 48.65 BBBB ATOM 2921 OD1 ASP B 44 −9.553 −53.026 − 17.753 1.00 50.52 BBBB ATOM 2922 OD2 ASP B 44 −8.791 −54.943 − 18.498 1.00 49.40 BBBB ATOM 2923 C ASP B 44 −6.236 −51.025 −19.598 1.00 44.13 BBBB ATOM 2924 O ASP B 44 −5.520 −50.968 −18.595 1.00 45.05 BBBB ATOM 2925 N ARG B 45 −6.001 −50.307 −20.692 1.00 42.34 BBBB ATOM 2926 CA ARG B 45 −4.887 −49.367 −20.763 1.00 40.44 BBBB ATOM 2927 CB ARG B 45 −3.802 −49.869 −21.725 1.00 41.87 BBBB ATOM 2928 CG ARG B 45 −2.935 −50.994 −21.149 1.00 43.86 BBBB ATOM 2929 CD ARG B 45 −2.218 −50.541 −19.881 1.00 45.24 BBBB ATOM 2930 NE ARG B 45 −1.385 −51.582 −19.277 1.00 46.96 BBBB ATOM 2931 CZ ARG B 45 −1.840 −52.753 −18.839 1.00 47.69 BBBB ATOM 2932 NH1 ARG B 45 − 3.130 −53.051 −18.937 1.00 48.59 BBBB ATOM 2933 NH2 ARG B 45 −1.005 −53.626 −18.289 1.00 48.33 BBBB ATOM 2934 C ARG B 45 −5.390 −47.992 −21.195 1.00 38.74 BBBB ATOM 2935 O ARG B 45 −6.486 −47.866 −21.738 1.00 37.69 BBBB ATOM 2936 N MET B 46 −4.567 −46.977 −20.955 1.00 37.09 BBBB ATOM 2937 CA MET B 46 −4.881 −45.581 −21.249 1.00 36.33 BBBB ATOM 2938 CB MET B 46 −3.644 −44.725 −20.945 1.00 37.92 BBBB ATOM 2939 CG MET B 46 −3.873 −43.222 −20.952 1.00 40.65 BBBB ATOM 2940 SD MET B 46 −3.420 −42.436 −22.517 1.00 44.22 BBBB ATOM 2941 CE MET B 46 −1.720 −41.959 −22.168 1.00 41.80 BBBB ATOM 2942 C MET B 46 −5.430 −45.239 −22.643 1.00 34.96 BBBB ATOM 2943 O MET B 46 −6.264 −44.338 −22.774 1.00 33.21 BBBB ATOM 2944 N GLU B 47 −4.976 −45.941 −23.678 1.00 32.85 BBBB ATOM 2945 CA GLU B 47 −5.458 −45.655 −25.029 1.00 31.79 BBBB ATOM 2946 CB GLU B 47 −4.624 −46.402 −26.080 1.00 30.62 BBBB ATOM 2947 CG GLU B 47 −4.755 −47.922 −26.051 1.00 29.85 BBBB ATOM 2948 CD GLU B 47 −3.793 −48.597 −25.082 1.00 29.78 BBBB ATOM 2949 OE1 GLU B 47 −3.188 −47.895 −24.247 1.00 28.76 BBBB ATOM 2950 OE2 GLU B 47 −3.649 −49.840 −25.156 1.00 29.01 BBBB ATOM 2951 C GLU B 47 −6.938 −46.017 −25.191 1.00 31.81 BBBB ATOM 2952 O GLU B 47 −7.626 −45.476 −26.055 1.00 31.31 BBBB ATOM 2953 N ALA B 48 −7.428 −46.924 −24.352 1.00 31.55 BBBB ATOM 2954 CA ALA B 48 −8.821 −47.344 −24.414 1.00 32.58 BBBB ATOM 2955 CB ALA B 48 −9.085 −48.450 −23.384 1.00 33.19 BBBB ATOM 2956 C ALA B 48 −9.761 −46.168 −24.164 1.00 33.37 BBBB ATOM 2957 C ALA B 48 −10.860 −46.114 −24.716 1.00 33.81 BBBB ATOM 2958 N ASP B 49 −9.328 −45.232 −23.328 1.00 34.05 BBBB ATOM 2959 CA ASP B 49 −10.143 −44.065 −23.009 1.00 35.60 BBBB ATOM 2960 CB ASP B 49 −10.033 −43.736 −21.514 1.00 36.58 BBBB ATOM 2961 CG ASP B 49 −10.645 −44.812 −20.628 1.00 39.54 BBBB ATOM 2962 OD1 ASP B 49 −11.835 −45.144 −20.825 1.00 40.82 BBBB ATOM 2963 OD2 ASP B 49 −9.939 −45.323 −19.730 1.00 39.49 BBBB ATOM 2964 C ASP B 49 −9.768 −42.832 −23.831 1.00 34.79 BBBB ATOM 2965 O ASP B 49 −10.637 −42.064 −24.241 1.00 35.85 BBBB ATOM 2966 N LEU B 50 −8.478 −42.648 −24.088 1.00 34.06 BBBB ATOM 2967 CA LEU B 50 −8.026 −41.484 −24.840 1.00 33.49 BBBB ATOM 2968 CB LEU B 50 −6.526 −41.264 −24.635 1.00 33.25 BBBB ATOM 2969 CG LEU B 50 −6.001 −39.986 −25.299 1.00 33.36 BBBB ATOM 2970 CD1 LEU B 50 −6.679 −38.771 −24.659 1.00 34.04 BBBB ATOM 2971 CD2 LEU B 50 −4.496 −39.894 −25.157 1.00 33.08 BBBB ATOM 2972 C LEU B 50 −8.320 −41.486 −26.337 1.00 33.52 BBBB ATOM 2973 O LEU B 50 −8.769 −40.477 −26.882 1.00 32.52 BBBB ATOM 2974 N VAL B 51 −8.073 −42.605 −27.011 1.00 32.94 BBBB ATOM 2975 CA VAL B 51 −8.299 −42.641 −28.449 1.00 32.68 BBBB ATOM 2976 CB VAL B 51 −7.829 −43.982 −29.058 1.00 33.06 BBBB ATOM 2977 CG1 VAL B 51 −8.115 −44.013 −30.565 1.00 31.54 BBBB ATOM 2978 CG2 VAL B 51 −6.329 −44.145 −28.813 1.00 31.45 BBBB ATOM 2979 C VAL B 51 −9.747 −42.348 −28.829 1.00 33.08 BBBB ATOM 2980 O VAL B 51 −10.000 −41.623 −29.792 1.00 32.88 BBBB ATOM 2981 N PRO B 52 −10.721 −42.900 −28.085 1.00 33.67 BBBB ATOM 2982 CD PRO B 52 −10.667 −44.012 −27.119 1.00 33.29 BBBB ATOM 2983 CA PRO B 52 −12.111 −42.601 −28.453 1.00 34.43 BBBB ATOM 2984 CB PRO B 52 −12.915 −43.465 −27.489 1.00 34.36 BBBB ATOM 2985 CG PRO B 52 −12.021 −44.661 −27.307 1.00 33.77 BBBB ATOM 2986 C PRO B 52 −12.422 −41.111 −28.294 1.00 35.67 BBBB ATOM 2987 O PRO B 52 −13.219 −40.548 −29.048 1.00 36.65 BBBB ATOM 2988 N LYS B 53 −11.790 −40.478 −27.310 1.00 35.75 BBBB ATOM 2989 CA LYS B 53 −11.998 −39.054 −27.064 1.00 36.73 BBBB ATOM 2990 CB LYS B 53 −11.334 −38.633 −25.746 1.00 37.14 BBBB ATOM 2991 CG LYS B 53 −12.020 −39.207 −24.514 1.00 38.38 BBBB ATOM 2992 CD LYS B 53 −11.368 −38.746 −23.218 1.00 39.34 BBBB ATOM 2993 CE LYS B 53 −12.057 −39.379 −22.012 1.00 40.74 BBBB ATOM 2994 NZ LYS B 53 −11.352 −39.092 −20.725 1.00 40.94 BBBB ATOM 2995 C LYS B 53 −11.445 −38.231 −28.220 1.00 36.11 BBBB ATOM 2996 O LYS B 53 −11.703 −37.036 −28.323 1.00 36.71 BBBB ATOM 2997 N HIS B 54 −10.688 −38.881 −29.096 1.00 35.60 BBBB ATOM 2998 CA HIS B 54 −10.116 −38.212 −30.259 1.00 34.62 BBBB ATOM 2999 CB HIS B 54 −8.666 −38.647 −30.464 1.00 34.78 BBBB ATOM 3000 CG HIS B 54 −7.676 −37.810 −29.721 1.00 33.79 BBBB ATOM 3001 CD2 HIS B 54 −7.360 −37.760 −28.406 1.00 33.76 BBBB ATOM 3002 ND1 HIS B 54 −6.884 −36.869 −30.343 1.00 34.27 BBBB ATOM 3003 CE1 HIS B 54 −6.120 −36.277 −29.441 1.00 34.41 BBBB ATOM 3004 NE2 HIS B 54 −6.390 −36.799 −28.258 1.00 33.91 BBBB ATOM 3005 C HIS B 54 −10.919 −38.524 −31.512 1.00 34.28 BBBB ATOM 3006 O HIS B 54 −10.487 −38.224 −32.620 1.00 34.99 BBBB ATOM 3007 N GLY B 55 −12.082 −39.140 −31.325 1.00 34.47 BBBB ATOM 3008 CA GLY B 55 −12.938 −39.481 −32.447 1.00 35.34 BBBB ATOM 3009 C GLY B 55 −12.427 −40.619 −33.310 1.00 36.18 BBBB ATOM 3010 O GLY B 55 −12.883 −40.799 −34.442 1.00 35.99 BBBB ATOM 3011 N ILE B 56 −11.490 −41.399 −32.776 1.00 35.32 BBBB ATOM 3012 CA ILE B 56 −10.909 −42.517 −33.514 1.00 33.81 BBBB ATOM 3013 CB ILE B 56 −9.374 −42.445 −33.462 1.00 33.36 BBBB ATOM 3014 CG2 ILE B 56 −8.761 −43.602 −34.245 1.00 32.87 BBBB ATOM 3015 CG1 ILE B 56 −8.916 −41.097 −34.029 1.00 32.05 BBBB ATOM 3016 CD1 ILE B 56 −7.461 −40.792 −33.818 1.00 30.35 BBBB ATOM 3017 C ILE B 56 −11.375 −43.859 −32.956 1.00 34.45 BBBB ATOM 3018 O ILE B 56 −11.394 −44.069 −31.738 1.00 34.26 BBBB ATOM 3019 N GLU B 57 −11.764 −44.758 −33.855 1.00 33.40 BBBB ATOM 3020 CA GLU B 57 −12.228 −46.083 −33.467 1.00 34.16 BBBB ATOM 3021 CB GLU B 57 −12.905 −46.769 −34.651 1.00 37.41 BBBB ATOM 3022 CG GLU B 57 −14.064 −45.982 −35.244 1.00 42.10 BBBB ATOM 3023 CD GLU B 57 −14.653 −46.659 −36.465 1.00 45.50 BBBB ATOM 3024 OE1 GLU B 57 −13.903 −46.875 −37.448 1.00 46.39 BBBB ATOM 3025 OE2 GLU B 57 −15.866 −46.977 −36.441 1.00 48.36 BBBB ATOM 3026 C GLU B 57 −11.044 −46.923 −33.005 1.00 33.01 BBBB ATOM 3027 O GLU B 57 −9.931 −46.769 −33.504 1.00 31.58 BBBB ATOM 3028 N ILE B 58 −11.287 −47.817 −32.056 1.00 31.85 BBBB ATOM 3029 CA ILE B 58 −10.217 −48.658 −31.553 1.00 31.38 BBBB ATOM 3030 CB ILE B 58 −9.651 −48.099 −30.223 1.00 30.95 BBBB ATOM 3031 CG2 ILE B 58 −10.769 −47.946 −29.205 1.00 31.48 BBBB ATOM 3032 CG1 ILE B 58 −8.553 −49.030 −29.690 1.00 31.13 BBBB ATOM 3033 CD1 ILE B 58 −7.736 −48.437 −28.572 1.00 29.87 BBBB ATOM 3034 C ILE B 58 −10.647 −50.102 −31.357 1.00 31.67 BBBB ATOM 3035 O ILE B 58 −11.716 −50.384 −30.801 1.00 30.68 BBBB ATOM 3036 N ASP B 59 −9.807 −51.011 −31.844 1.00 30.76 BBBB ATOM 3037 CA ASP B 59 −10.039 −52.442 −31.720 1.00 31.09 BBBB ATOM 3038 CB ASP B 59 −9.732 −53.153 −33.037 1.00 31.37 BBBB ATOM 3039 CG ASP B 59 −10.766 −52.863 −34.104 1.00 32.68 BBBB ATOM 3040 OD1 ASP B 59 −11.969 −53.037 −33.812 1.00 32.40 BBBB ATOM 3041 OD2 ASP B 59 −10.378 −52.468 −35.224 1.00 33.40 BBBB ATOM 3042 C ASP B 59 −9.119 −52.950 −30.618 1.00 30.50 BBBB ATOM 3043 O ASP B 59 −7.987 −52.491 −30.492 1.00 30.24 BBBB ATOM 3044 N PHE B 60 −9.608 −53.888 −29.815 1.00 30.65 BBBB ATOM 3045 CA PHE B 60 −8.809 −54.410 −28.713 1.00 30.32 BBBB ATOM 3046 CB PHE B 60 −9.560 −54.239 −27.385 1.00 30.74 BBBB ATOM 3047 CG PHE B 60 −9.925 −52.815 −27.058 1.00 32.14 BBBB ATOM 3048 CD1 PHE B 60 −11.250 −52.392 −27.129 1.00 33.15 BBBB ATOM 3049 CD2 PHE B 60 −8.955 −51.908 −26.649 1.00 31.57 BBBB ATOM 3050 CE1 PHE B 60 −11.605 −51.083 −26.791 1.00 34.05 BBBB ATOM 3051 CE2 PHE B 60 −9.294 −50.598 −26.310 1.00 33.00 BBBB ATOM 3052 CZ PHE B 60 −10.626 −50.185 −26.380 1.00 33.82 BBBB ATOM 3053 C PHE B 60 −8.430 −55.878 −28.846 1.00 29.86 BBBB ATOM 3054 O PHE B 60 −9.154 −56.668 −29.445 1.00 29.93 BBBB ATOM 3055 N ILE B 61 −7.271 −56.229 −28.295 1.00 29.38 BBBB ATOM 3056 CA ILE B 61 −6.832 −57.616 −28.269 1.00 28.55 BBBB ATOM 3057 CB ILE B 61 −5.674 −57.923 −29.258 1.00 28.48 BBBB ATOM 3058 CG2 ILE B 61 −6.123 −57.650 −30.694 1.00 27.65 BBBB ATOM 3059 CG1 ILE B 61 −4.422 −57.126 −28.892 1.00 26.70 BBBB ATOM 3060 CD1 ILE B 61 −3.177 −57.615 −29.638 1.00 27.03 BBBB ATOM 3061 C ILE B 61 −6.344 −57.855 −26.848 1.00 29.13 BBBB ATOM 3062 O ILE B 61 −6.124 −56.906 −26.091 1.00 28.80 BBBB ATOM 3063 N ARG B 62 −6.186 −59.116 −26.473 1.00 29.38 BBBB ATOM 3064 CA ARG B 62 −5.709 −59.416 −25.133 1.00 30.76 BBBB ATOM 3065 CB ARG B 62 −6.630 −60.447 −24.461 1.00 32.36 BBBB ATOM 3066 CG ARG B 62 −6.130 −60.955 −23.114 1.00 35.99 BBBB ATOM 3067 CD ARG B 62 −5.438 −59.859 −22.311 1.00 37.86 BBBB ATOM 3068 NE ARG B 62 −6.297 −58.718 −22.004 1.00 40.01 BBBB ATOM 3069 CZ ARG B 62 −5.840 −57.504 −21.711 1.00 39.09 BBBB ATOM 3070 NH1 ARG B 62 −4.536 −57.275 −21.690 1.00 39.24 BBBB ATOM 3071 NH2 ARG B 62 −6.686 −56.518 −21.439 1.00 40.03 BBBB ATOM 3072 C ARG B 62 −4.274 −59.923 −25.156 1.00 29.32 BBBB ATOM 3073 O ARG B 62 −3.933 −60.809 −25.934 1.00 28.65 BBBB ATOM 3074 N ILE B 63 −3.428 −59.342 −24.313 1.00 30.07 BBBB ATOM 3075 CA ILE B 63 −2.036 −59.770 −24.231 1.00 31.38 BBBB ATOM 3076 CB ILE B 63 −1.081 −58.745 −24.883 1.00 30.06 BBBB ATOM 3077 CG2 ILE B 63 −1.442 −58.567 −26.353 1.00 30.41 BBBB ATOM 3078 CG1 ILE B 63 −1.143 −57.411 −24.137 1.00 29.94 BBBB ATOM 3079 CD1 ILE B 63 −0.128 −56.384 −24.632 1.00 29.62 BBBB ATOM 3080 C ILE B 63 −1.623 −59.981 −22.775 1.00 33.08 BBBB ATOM 3081 O ILE B 63 −0.444 −59.872 −22.430 1.00 33.21 BBBB ATOM 3082 N SER B 64 −2.603 −60.284 −21.927 1.00 35.38 BBBB ATOM 3083 CA SER B 64 −2.356 −60.520 − 20.505 1.00 37.51 BBBB ATOM 3084 CB SER B 64 −3.652 −60.912 − 19.792 1.00 38.82 BBBB ATOM 3085 OG SER B 64 −4.558 −59.823 − 19.750 1.00 42.88 BBBB ATOM 3086 C SER B 64 −1.326 −61.622 − 20.311 1.00 37.32 BBBB ATOM 3087 O SER B 64 −1.411 −62.682 − 20.933 1.00 37.86 BBBB ATOM 3088 N GLY B 65 −0.356 −61.370 − 19.441 1.00 37.81 BBBB ATOM 3089 CA GLY B 65 0.679 −62.355 − 19.199 1.00 37.13 BBBB ATOM 3090 C GLY B 65 1.798 −62.283 − 20.226 1.00 36.26 BBBB ATOM 3091 O GLY B 65 2.858 −62.889 − 20.038 1.00 37.57 BBBB ATOM 3092 N LEU B 66 1.577 −61.539 −21.307 1.00 34.63 BBBB ATOM 3093 CA LEU B 66 2.591 −61.413 −22.355 1.00 33.17 BBBB ATOM 3094 CB LEU B 66 1.936 −61.470 −23.735 1.00 32.08 BBBB ATOM 3095 CG LEU B 66 1.162 −62.747 −24.061 1.00 32.52 BBBB ATOM 3096 CD1 LEU B 66 0.563 −62.626 −25.445 1.00 31.38 BBBB ATOM 3097 CD2 LEU B 66 2.093 −63.957 −23.984 1.00 31.67 BBBB ATOM 3098 C LEU B 66 3.414 −60.133 −22.246 1.00 32.72 BBBB ATOM 3099 O LEU B 66 4.451 −60.002 −22.893 1.00 33.13 BBBB ATOM 3100 N ARG B 67 2.953 −59.185 −21.440 1.00 31.54 BBBB ATOM 3101 CA ARG B 67 3.671 −57.928 −21.277 1.00 30.90 BBBB ATOM 3102 CB ARG B 67 2.888 −56.984 − 20.363 1.00 32.28 BBBB ATOM 3103 CG ARG B 67 1.540 −56.576 − 20.913 1.00 34.65 BBBB ATOM 3104 CD ARG B 67 0.926 −55.440 − 20.097 1.00 36.69 BBBB ATOM 3105 NE ARG B 67 −0.259 −54.889 − 20.748 1.00 38.28 BBBB ATOM 3106 CZ ARG B 67 −1.425 −55.519 −20.853 1.00 39.05 BBBB ATOM 3107 NH1 ARG B 62 −1.583 −56.734 −20.341 1.00 39.61 BBBB ATOM 3108 NH2 ARG B 67 −2.434 −54.935 −21.487 1.00 39.52 BBBB ATOM 3109 C ARG B 67 5.071 −58.142 − 20.713 1.00 29.99 BBBB ATOM 3110 O ARG B 67 5.294 −59.034 − 19.889 1.00 28.67 BBBB ATOM 3111 N GLY B 68 6.014 −57.321 −21.165 1.00 27.75 BBBB ATOM 3112 CA GLY B 68 7.380 −57.427 − 20.685 1.00 26.79 BBBB ATOM 3113 C GLY B 68 8.166 −58.579 −21.280 1.00 25.41 BBBB ATOM 3114 O GLY B 68 9.326 −58.779 −20.943 1.00 26.04 BBBB ATOM 3115 N LYS B 69 7.546 −59.342 −22.170 1.00 24.55 BBBB ATOM 3116 CA LYS B 69 8.238 −60.463 −22.796 1.00 23.93 BBBB ATOM 3117 CB LYS B 69 7.284 −61.641 −23.033 1.00 24.12 BBBB ATOM 3118 CG LYS B 69 6.757 −62.360 −21.794 1.00 25.08 BBBB ATOM 3119 CD LYS B 69 5.887 −63.553 −22.224 1.00 25.44 BBBB ATOM 3120 CE LYS B 69 5.357 −64.358 −21.035 1.00 28.31 BBBB ATOM 3121 NZ LYS B 69 6.468 −64.877 −20.175 1.00 29.71 BBBB ATOM 3122 C LYS B 69 8.825 −60.062 −24.142 1.00 23.32 BBBB ATOM 3123 O LYS B 69 8.151 −59.404 −24.944 1.00 21.96 BBBB ATOM 3124 N GLY B 70 10.075 −60.470 −24.374 1.00 22.48 BBBB ATOM 3125 CA GLY B 70 10.755 −60.229 −25.636 1.00 22.26 BBBB ATOM 3126 C GLY B 70 10.308 −61.337 −26.588 1.00 22.17 BBBB ATOM 3127 O GLY B 70 9.512 −62.183 −26.195 1.00 21.62 BBBB ATOM 3128 N ILE B 71 10.819 −61.373 −27.814 1.00 21.85 BBBB ATOM 3129 CA ILE B 71 10.357 −62.386 −28.762 1.00 23.55 BBBB ATOM 3130 CB ILE B 71 10.926 −62.142 −30.181 1.00 23.52 BBBB ATOM 3131 CG2 ILE B 71 12.435 −62.375 −30.192 1.00 25.96 BBBB ATOM 3132 CG1 ILE B 71 10.264 −63.096 −31.182 1.00 24.18 BBBB ATOM 3133 CD1 ILE B 71 8.745 −62.981 −31.263 1.00 25.73 BBBB ATOM 3134 C ILE B 71 10.616 −63.840 −28.359 1.00 23.88 BBBB ATOM 3135 O ILE B 71 9.775 −64.707 −28.592 1.00 21.66 BBBB ATOM 3136 N LYS B 72 11.764 −64.119 −27.751 1.00 23.82 BBBB ATOM 3137 CA LYS B 72 12.038 −65.491 −27.343 1.00 24.92 BBBB ATOM 3138 CB LYS B 72 13.491 −65.634 −26.875 1.00 26.86 BBBB ATOM 3139 CG LYS B 72 14.496 −65.590 −28.019 1.00 31.29 BBBB ATOM 3140 CD LYS B 72 15.925 −65.791 −27.518 1.00 36.00 BBBB ATOM 3141 CE LYS B 72 16.926 −65.816 −28.671 1.00 38.82 BBBB ATOM 3142 NZ LYS B 72 18.342 −65.957 −28.192 1.00 41.21 BBBB ATOM 3143 C LYS B 72 11.068 −65.925 −26.245 1.00 23.73 BBBB ATOM 3144 O LYS B 72 10.592 −67.062 −26.245 1.00 24.08 BBBB ATOM 3145 N ALA B 73 10.765 −65.016 −25.322 1.00 21.62 BBBB ATOM 3146 CA ALA B 73 9.839 −65.306 −24.233 1.00 21.18 BBBB ATOM 3147 CB ALA B 73 9.895 −64.196 −23.187 1.00 22.25 BBBB ATOM 3148 C ALA B 73 8.412 −65.454 −24.771 1.00 20.36 BBBB ATOM 3149 O ALA B 73 7.619 −66.250 −24.267 1.00 18.97 BBBB ATOM 3150 N LEU B 74 8.076 −64.673 −25.791 1.00 20.23 BBBB ATOM 3151 CA LEU B 74 6.745 −64.762 −26.387 1.00 19.36 BBBB ATOM 3152 CB LEU B 74 6.540 −63.643 −27.417 1.00 18.42 BBBB ATOM 3153 CG LEU B 74 6.422 −62.208 −26.884 1.00 18.80 BBBB ATOM 3154 CD1 LEU B 74 6.473 −61.197 −28.039 1.00 19.86 BBBB ATOM 3155 CD2 LEU B 74 5.109 −62.071 −26.104 1.00 19.45 BBBB ATOM 3156 C LEU B 74 6.549 −66.110 −27.069 1.00 19.37 BBBB ATOM 3157 O LEU B 74 5.539 −66.779 −26.863 1.00 20.01 BBBB ATOM 3158 N ILE B 75 7.520 −66.507 −27.883 1.00 20.59 BBBB ATOM 3159 CA ILE B 75 7.434 −67.768 −28.601 1.00 21.18 BBBB ATOM 3160 CB ILE B 75 8.571 −67.896 −29.641 1.00 22.95 BBBB ATOM 3161 CG2 ILE B 75 8.334 −69.108 −30.527 1.00 25.38 BBBB ATOM 3162 CG1 ILE B 75 8.598 −66.657 −30.540 1.00 26.82 BBBB ATOM 3163 CD1 ILE B 75 7.304 −66.442 −31.327 1.00 28.48 BBBB ATOM 3164 C ILE B 75 7.488 −68.942 −27.624 1.00 21.20 BBBB ATOM 3165 O ILE B 75 7.125 −70.063 −27.979 1.00 21.59 BBBB ATOM 3166 N ALA B 76 7.940 −68.680 −2.399 1.00 20.49 BBBB ATOM 3167 CA ALA B 76 7.996 −69.726 −25.374 1.00 21.72 BBBB ATOM 3168 CB ALA B 76 9.026 −69.372 −24.305 1.00 21.92 BBBB ATOM 3169 C ALA B 76 6.624 −69.904 −24.732 1.00 21.54 BBBB ATOM 3170 O ALA B 76 6.441 −70.778 −23.875 1.00 20.75 BBBB ATOM 3171 N ALA B 77 5.668 −69.066 −25.145 1.00 20.61 BBBB ATOM 3172 CA ALA B 77 4.289 −69.121 −24.655 1.00 21.07 BBBB ATOM 3173 CB ALA B 77 3.937 −67.830 −23.924 1.00 20.10 BBBB ATOM 3174 C ALA B 77 3.383 −69.298 −25.881 1.00 21.69 BBBB ATOM 3175 O ALA B 77 2.567 −68.430 −26.199 1.00 21.93 BBBB ATOM 3176 N PRO B 78 3.507 −70.446 −26.564 1.00 22.38 BBBB ATOM 3177 CD PRO B 78 4.211 −71.603 −25.976 1.00 21.89 BBBB ATOM 3178 CA PRO B 78 2.772 −70.846 −27.771 1.00 20.95 BBBB ATOM 3179 CB PRO B 78 3.027 −72.350 −27.861 1.00 22.21 BBBB ATOM 3180 CG PRO B 78 4.288 −72.547 −27.117 1.00 24.07 BBBB ATOM 3181 C PRO B 78 1.278 −70.535 −27.813 1.00 21.19 BBBB ATOM 3182 O PRO B 78 0.789 −69.939 −28.776 1.00 19.68 BBBB ATOM 3183 N LEU B 79 0.544 −70.961 −26.790 1.00 21.21 BBBB ATOM 3184 CA LEU B 79 − 0.896 −70.728 −26.783 1.00 21.32 BBBB ATOM 3185 CB LEU B 79 −1.569 −71.476 −25.630 1.00 20.99 BBBB ATOM 3186 CG LEU B 79 −1.397 −72.988 −25.617 1.00 22.40 BBBB ATOM 3187 CD1 LEU B 79 −2.504 −73.619 −24.772 1.00 22.01 BBBB ATOM 3188 CD2 LEU B 79 −1.438 −73.521 −27.021 1.00 23.82 BBBB ATOM 3189 C LEU B 79 −1.275 −69.263 −26.707 1.00 21.17 BBBB ATOM 3190 O LEU B 79 −2.125 −68.800 −27.481 1.00 20.44 BBBB ATOM 3191 N ARG B 80 −0.656 −68.529 −25.788 1.00 20.91 BBBB ATOM 3192 CA ARG B 80 −0.980 −67.115 −25.637 1.00 21.30 BBBB ATOM 3193 CB ARG B 80 −0.444 −66.583 −24.312 1.00 22.12 BBBB ATOM 3194 CG ARG B 80 −1.286 −67.051 −23.118 1.00 24.03 BBBB ATOM 3195 CD ARG B 80 −0.610 −66.738 −21.807 1.00 23.42 BBBB ATOM 3196 NE ARG B 80 0.581 −67.556 −21.610 1.00 24.59 BBBB ATOM 3197 CZ ARG B 80 1.466 −67.351 −20.642 1.00 26.08 BBBB ATOM 3198 NH1 ARG B 80 1.290 −66.349 −19.787 1.00 26.92 BBBB ATOM 3199 NH2 ARG B 80 2.514 −68.152 −20.519 1.00 27.22 BBBB ATOM 3200 C ARG B 80 −0.526 −66.233 −26.790 1.00 21.29 BBBB ATOM 3201 O ARG B 80 −1.278 −65.355 −27.223 1.00 21.47 BBBB ATOM 3202 N ILE B 81 0.683 −66.448 −27.303 1.00 19.29 BBBB ATOM 3203 CA ILE B 81 1.113 −65.621 −28.421 1.00 19.47 BBBB ATOM 3204 CB ILE B 81 2.639 −65.793 −28.730 1.00 17.92 BBBB ATOM 3205 CG2 ILE B 81 2.949 −67.200 −29.206 1.00 17.33 BBBB ATOM 3206 CG1 ILE B 81 3.067 −64.753 −29.769 1.00 18.63 BBBB ATOM 3207 CD1 ILE B 81 2.746 −63.318 −29.346 1.00 17.46 BBBB ATOM 3208 C ILE B 81 0.256 −65.937 −29.654 1.00 18.99 BBBB ATOM 3209 O ILE B 81 −0.149 −65.028 −30.378 1.00 19.38 BBBB ATOM 3210 N PHE B 82 −0.056 −67.211 −29.880 1.00 19.39 BBBB ATOM 3211 CA PHE B 82 −0.875 −67.582 −31.038 1.00 19.15 BBBB ATOM 3212 CB PHE B 82 −1.057 −69.103 −31.136 1.00 19.27 BBBB ATOM 3213 CG PHE B 82 −1.811 −69.548 −32.368 1.00 19.87 BBBB ATOM 3214 CD1 PHE B 82 −1.180 −69.602 −33.603 1.00 20.87 BBBB ATOM 3215 CD2 PHE B 82 −3.154 −69.898 −32.289 1.00 21.11 BBBB ATOM 3216 CE1 PHE B 82 −1.872 −70.002 −34.753 1.00 21.20 BBBB ATOM 3217 CE2 PHE B 82 −3.857 −70.297 −33.429 1.00 22.26 BBBB ATOM 3218 CZ PHE B 82 −3.212 −70.349 −34.663 1.00 22.14 BBBB ATOM 3219 C PHE B 82 −2.250 −66.931 −30.959 1.00 19.94 BBBB ATOM 3220 O PHE B 82 −2.777 −66.444 −31.970 1.00 19.64 BBBB ATOM 3221 N ASN B 83 −2.832 −66.923 −29.764 1.00 19.29 BBBB ATOM 3222 CA ASN B 83 −4.150 −66.332 −29.577 1.00 20.90 BBBB ATOM 3223 CB ASN B 83 −4.693 −66.641 −28.178 1.00 20.55 BBBB ATOM 3224 CG ASN B 83 −6.158 −66.244 −28.028 1.00 22.79 BBBB ATOM 3225 OD1 ASN B 83 −6.505 −65.374 −27.229 1.00 25.14 BBBB ATOM 3226 ND2 ASN B 83 −7.018 −66.877 −28.807 1.00 20.47 BBBB ATOM 3227 C ASN B 83 −4.178 −64.821 −29.812 1.00 20.83 BBBB ATOM 3228 O ASN B 83 −5.086 −64.316 −30.472 1.00 21.92 BBBB ATOM 3229 N ALA B 84 −3.203 −64.092 −29.275 1.00 19.74 BBBB ATOM 3230 CA ALA B 84 −3.177 −62.647 −29.484 1.00 19.30 BBBB ATOM 3231 CB ALA B 84 −2.060 −62.008 −28.662 1.00 18.59 BBBB ATOM 3232 C ALA B 84 −2.967 −62.380 −30.981 1.00 19.94 BBBB ATOM 3233 O ALA B 84 −3.561 −61.459 −31.552 1.00 19.69 BBBB ATOM 3234 N TRP B 85 −2.118 −63.197 −31.603 1.00 19.77 BBBB ATOM 3235 CA TRP B 85 −1.820 −63.111 −33.032 1.00 20.56 BBBB ATOM 3236 CB TRP B 85 −0.754 −64.148 −33.396 1.00 21.46 BBBB ATOM 3237 CG TRP B 85 −0.365 −64.167 −34.856 1.00 23.00 BBBB ATOM 3238 CD2 TRP B 85 −0.588 −65.232 −35.785 1.00 23.69 BBBB ATOM 3239 CE2 TRP B 85 −0.024 −64.835 −37.022 1.00 24.14 BBBB ATOM 3240 CE3 TRP B 85 −1.206 −66.486 −35.693 1.00 24.79 BBBB ATOM 3241 CD1 TRP B 85 0.301 −63.189 −35.548 1.00 23.17 BBBB ATOM 3242 NE1 TRP B 85 0.509 −63.585 −36.848 1.00 24.28 BBBB ATOM 3243 CZ2 TRP B 85 −0.060 −65.650 −38.160 1.00 24.90 BBBB ATOM 3244 CZ3 TRP B 85 −1.243 −67.299 −36.827 1.00 25.45 BBBB ATOM 3245 CH2 TRP B 85 −0.671 −66.875 −38.045 1.00 25.15 BBBB ATOM 3246 C TRP B 85 −3.090 −63.354 −33.865 1.00 21.76 BBBB ATOM 3247 O TRP B 85 −3.339 −62.658 −34.859 1.00 20.40 BBBB ATOM 3248 N ARG B 86 −3.885 −64.346 −33.467 1.00 22.03 BBBB ATOM 3249 CA ARG B 86 −5.140 −64.660 −34.166 1.00 23.28 BBBB ATOM 3250 CB ARG B 86 −5.754 −65.965 −33.623 1.00 24.72 BBBB ATOM 3251 CG ARG B 86 −4.999 −67.236 −34.021 1.00 27.21 BBBB ATOM 3252 CD ARG B 86 −5.368 −67.725 −35.418 1.00 29.60 BBBB ATOM 3253 NE ARG B 86 −6.626 −68.477 −35.422 1.00 31.45 BBBB ATOM 3254 CZ ARG B 86 −7.185 −69.004 −36.508 1.00 31.37 BBBB ATOM 3255 NH1 ARG B 86 −6.607 −68.862 −37.696 1.00 32.19 BBBB ATOM 3256 NH2 ARG B 86 −8.314 −69.694 −36.405 1.00 31.39 BBBB ATOM 3257 C ARG B 86 −6.151 −63.517 −34.007 1.00 22.98 BBBB ATOM 3258 O ARG B 86 −6.890 −63.195 −34.942 1.00 21.37 BBBB ATOM 3259 N GLN B 87 −6.190 −62.916 −32.821 1.00 22.90 BBBB ATOM 3260 CA GLN B 87 −7.101 −61.802 −32.567 1.00 24.07 BBBB ATOM 3261 CB GLN B 87 −7.046 −61.382 −31.097 1.00 24.33 BBBB ATOM 3262 CG GLN B 87 −7.873 −62.280 −30.187 1.00 27.24 BBBB ATOM 3263 CD GLN B 87 −7.720 −61.943 −28.723 1.00 28.81 BBBB ATOM 3264 OE1 GLN B 87 −8.567 −62.296 −27.908 1.00 33.25 BBBB ATOM 3265 NE2 GLN B 87 −6.632 −61.275 −28.375 1.00 29.95 BBBB ATOM 3266 C GLN B 87 −6.738 −60.618 −33.457 1.00 23.85 BBBB ATOM 3267 O GLN B 87 −7.613 −60.012 −34.077 1.00 24.02 BBBB ATOM 3268 N ALA B 88 −5.449 −60.293 −33.521 1.00 23.39 BBBB ATOM 3269 CA ALA B 88 −4.996 −59.183 −34.355 1.00 23.78 BBBB ATOM 3270 CB ALA B 88 −3.508 −58.909 −34.116 1.00 23.33 BBBB ATOM 3271 C ALA B 88 −5.257 −59.485 −35.831 1.00 24.73 BBBB ATOM 3272 O ALA B 88 −5.655 −58.595 −36.592 1.00 24.72 BBBB ATOM 3273 N ARG B 89 −5.038 −60.735 −36.244 1.00 24.26 BBBB ATOM 3274 CA ARG B 89 −5.285 −61.111 −37.636 1.00 24.94 BBBB ATOM 3275 CB ARG B 89 −4.904 −62.575 −37.893 1.00 25.14 BBBB ATOM 3276 CG ARG B 89 −3.461 −62.774 −38.353 1.00 24.54 BBBB ATOM 3277 CD ARG B 89 −3.142 −64.253 −38.510 1.00 25.50 BBBB ATOM 3278 NE ARG B 89 −3.809 −64.901 −39.641 1.00 24.93 BBBB ATOM 3279 CZ ARG B 89 −3.329 −64.930 −40.882 1.00 25.90 BBBB ATOM 3280 NH1 ARG B 89 −2.178 −64.336 −41.170 1.00 25.98 BBBB ATOM 3281 NH2 ARG B 89 −3.979 −65.596 −41.831 1.00 26.36 BBBB ATOM 3282 C ARG B 89 −6.752 −60.909 −38.013 1.00 25.29 BBBB ATOM 3283 O ARG B 89 −7.056 −60.420 −39.104 1.00 24.27 BBBB ATOM 3284 N ALA B 90 −7.658 −61.296 −37.118 1.00 24.61 BBBB ATOM 3285 CA ALA B 90 −9.088 −61.151 −37.383 1.00 26.16 BBBB ATOM 3286 CB ALA B 90 −9.907 −61.775 −36.254 1.00 25.77 BBBB ATOM 3287 C ALA B 90 −9.440 −59.673 −37.538 1.00 26.83 BBBB ATOM 3288 O ALA B 90 −10.213 −59.301 −38.421 1.00 27.71 BBBB ATOM 3289 N ILE B 91 −8.862 −58.837 −36.685 1.00 26.92 BBBB ATOM 3290 CA ILE B 91 − 9.108 −57.400 −36.733 1.00 26.97 BBBB ATOM 3291 CB ILE B 91 −8.408 −56.682 −35.565 1.00 27.03 BBBB ATOM 3292 CG2 ILE B 91 −8.327 −55.175 −35.837 1.00 25.82 BBBB ATOM 3293 CG1 ILE B 91 −9.161 −56.962 −34.260 1.00 24.58 BBBB ATOM 3294 CD1 ILE B 91 −8.435 −56.490 −33.021 1.00 24.65 BBBB ATOM 3295 C ILE B 91 −8.618 −56.787 −38.040 1.00 28.07 BBBB ATOM 3296 O ILE B 91 −9.289 −55.934 −38.629 1.00 28.41 BBBB ATOM 3297 N MET B 92 −7.451 −57.227 −38.496 1.00 27.92 BBBB ATOM 3298 CA MET B 92 −6.872 −56.693 −39.717 1.00 29.03 BBBB ATOM 3299 CB MET B 92 −5.366 −56.912 −39.712 1.00 27.34 BBBB ATOM 3300 CG MET B 92 −4.686 −56.235 −38.536 1.00 26.09 BBBB ATOM 3301 SD MET B 92 −2.919 −56.413 −38.602 1.00 25.72 BBBB ATOM 3302 CE MET B 92 −2.413 −55.394 −37.218 1.00 24.09 BBBB ATOM 3303 C MET B 92 −7.488 −57.257 −40.988 1.00 30.07 BBBB ATOM 3304 O MET B 92 −7.417 −56.628 −42.046 1.00 30.66 BBBB ATOM 3305 N LYS B 93 −8.082 −58.441 −40.894 1.00 30.96 BBBB ATOM 3306 CA LYS B 93 −8.735 −59.038 −42.050 1.00 33.20 BBBB ATOM 3307 CB LYS B 93 −8.969 −60.537 −41.826 1.00 34.31 BBBB ATOM 3308 CG LYS B 93 −7.689 −61.369 −41.860 1.00 36.71 BBBB ATOM 3309 CD LYS B 93 −7.956 −62.847 −41.576 1.00 38.43 BBBB ATOM 3310 CE LYS B 93 −8.781 −63.491 −42.683 1.00 38.82 BBBB ATOM 3311 NZ LYS B 93 −9.197 −64.881 −42.344 1.00 40.70 BBBB ATOM 3312 C LYS B 93 −10.067 −58.314 −42.252 1.00 33.65 BBBB ATOM 3313 O LYS B 93 −10.524 −58.143 −43.382 1.00 34.76 BBBB ATOM 3314 N ALA B 94 −10.672 −57.877 −41.147 1.00 33.00 BBBB ATOM 3315 CA ALA B 94 −11.943 −57.157 −41.183 1.00 33.62 BBBB ATOM 3316 CB ALA B 94 −12.641 −57.260 −39.833 1.00 33.62 BBBB ATOM 3317 C ALA B 94 −11.752 −55.684 −41.559 1.00 33.95 BBBB ATOM 3318 O ALA B 94 −12.484 −55.153 −42.397 1.00 33.20 BBBB ATOM 3319 N TYR B 95 −10.772 −55.028 −40.943 1.00 33.15 BBBB ATOM 3320 CA TYR B 95 −10.504 −53.620 −41.224 1.00 33.83 BBBB ATOM 3321 CB TYR B 95 −9.722 −52.992 −40.060 1.00 33.92 BBBB ATOM 3322 CG TYR B 95 −9.383 −51.525 −40.249 1.00 34.38 BBBB ATOM 3323 CD1 TYR B 95 −10.381 −50.585 −40.499 1.00 36.04 BBBB ATOM 3324 CE1 TYR B 95 −10.071 −49.240 −40.702 1.00 36.49 BBBB ATOM 3325 CD2 TYR B 95 −8.063 −51.082 −40.202 1.00 34.89 BBBB ATOM 3326 CE2 TYR B 95 −7.741 −49.741 −40.401 1.00 35.72 BBBB ATOM 3327 CZ TYR B 95 −8.750 −48.826 −40.655 1.00 36.79 BBBB ATOM 3328 OH TYR B 95 −8.436 −47.502 −40.874 1.00 37.60 BBBB ATOM 3329 C TYR B 95 −9.743 −53.418 −42.538 1.00 34.06 BBBB ATOM 3330 O TYR B 95 −9.919 −52.404 −43.214 1.00 33.85 BBBB ATOM 3331 N LYS B 96 −8.902 −54.386 −42.896 1.00 33.76 BBBB ATOM 3332 CA LYS B 96 −8.104 −54.327 −44.122 1.00 33.85 BBBB ATOM 3333 CB LYS B 96 −9.004 −54.476 −45.353 1.00 35.14 BBBB ATOM 3334 CG LYS B 96 −9.707 −55.812 −45.463 1.00 37.16 BBBB ATOM 3335 CD LYS B 96 −10.649 −55.843 −46.661 1.00 38.58 BBBB ATOM 3336 CE LYS B 96 −11.388 −57.170 −46.752 1.00 40.07 BBBB ATOM 3337 NZ LYS B 96 −12.319 −57.218 −47.925 1.00 41.29 BBBB ATOM 3338 C LYS B 96 −7.278 −53.049 −44.262 1.00 33.75 BBBB ATOM 3339 O LYS B 96 −7.489 −52.258 −45.189 1.00 34.55 BBBB ATOM 3340 N PRO B 97 −6.326 −52.825 −43.345 1.00 32.59 BBBB ATOM 3341 CD PRO B 97 −6.004 −53.620 −42.143 1.00 32.37 BBBB ATOM 3342 CA PRO B 97 −5.490 −51.623 −43.419 1.00 31.82 BBBB ATOM 3343 CB PRO B 97 −4.850 −51.568 −42.038 1.00 31.66 BBBB ATOM 3344 CG PRO B 97 −4.686 −53.025 −41.704 1.00 31.53 BBBB ATOM 3345 C PRO B 97 −4.458 −51.769 −44.530 1.00 31.60 BBBB ATOM 3346 O PRO B 97 −4.052 −52.881 −44.860 1.00 32.52 BBBB ATOM 3347 N ASP B 98 −4.037 −50.651 −45.112 1.00 31.25 BBBB ATOM 3348 CA ASP B 98 −3.049 −50.685 −46.188 1.00 29.78 BBBB ATOM 3349 CB ASP B 98 −3.234 −49.488 −47.117 1.00 32.00 BBBB ATOM 3350 CG ASP B 98 −4.562 −49.519 −47.837 1.00 34.21 BBBB ATOM 3351 OD1 ASP B 98 −5.281 −48.498 −47.795 1.00 35.37 BBBB ATOM 3352 OD2 ASP B 98 −4.888 −50.566 −48.443 1.00 35.10 BBBB ATOM 3353 C ASP B 98 −1.654 −50.660 −45.603 1.00 28.70 BBBB ATOM 3354 O ASP B 98 −0.672 −50.973 −46.274 1.00 26.48 BBBB ATOM 3355 N VAL B 99 −1.573 −50.278 −44.337 1.00 26.88 BBBB ATOM 3356 CA VAL B 99 −0.296 −50.214 −43.660 1.00 26.75 BBBB ATOM 3357 CB VAL B 99 0.500 −48.973 −44.132 1.00 27.35 BBBB ATOM 3358 CG1 VAL B 99 −0.305 −47.718 −43.867 1.00 29.45 BBBB ATOM 3359 CG2 VAL B 99 1.841 −48.908 −43.443 1.00 27.48 BBBB ATOM 3360 C VAL B 99 −0.552 −50.134 −42.162 1.00 25.92 BBBB ATOM 3361 O VAL B 99 −1.585 −49.627 −41.723 1.00 25.04 BBBB ATOM 3362 N VAL B 100 0.374 −50.664 −41.377 1.00 24.63 BBBB ATOM 3363 CA VAL B 100 0.227 −50.613 −39.936 1.00 23.59 BBBB ATOM 3364 CB VAL B 100 0.120 −52.026 −39.327 1.00 24.97 BBBB ATOM 3365 CG1 VAL B 100 0.139 −51.941 −37.811 1.00 24.71 BBBB ATOM 3366 CG2 VAL B 100 −1.172 −52.683 −39.782 1.00 22.62 BBBB ATOM 3367 C VAL B 100 1.428 −49.881 −39.382 1.00 22.74 BBBB ATOM 3368 O VAL B 100 2.551 −50.093 −39.830 1.00 24.62 BBBB ATOM 3369 N LEU B 101 1.178 −49.001 −38.419 1.00 21.89 BBBB ATOM 3370 CA LEU B 101 2.214 −48.199 −37.797 1.00 21.59 BBBB ATOM 3371 CB LEU B 101 1.823 −46.716 −37.853 1.00 22.86 BBBB ATOM 3372 CG LEU B 101 2.850 −45.580 −37.892 1.00 24.72 BBBB ATOM 3373 CD1 LEU B 101 2.237 −44.385 −37.174 1.00 25.30 BBBB ATOM 3374 CD2 LEU B 101 4.168 −45.954 −37.273 1.00 24.45 BBBB ATOM 3375 C LEU B 101 2.349 −48.604 −36.336 1.00 20.83 BBBB ATOM 3376 O LEU B 101 1.370 −48.581 −35.595 1.00 21.35 BBBB ATOM 3377 N GLY B 102 3.556 −48.986 −35.936 1.00 20.96 BBBB ATOM 3378 CA GLY B 102 3.796 −49.357 −34.549 1.00 19.23 BBBB ATOM 3379 C GLY B 102 4.655 −48.282 −33.918 1.00 18.45 BBBB ATOM 3380 O GLY B 102 5.765 −48.016 −34.381 1.00 18.70 BBBB ATOM 3381 N MET B 103 4.155 −47.660 −32.857 1.00 18.01 BBBB ATOM 3382 CA MET B 103 4.892 −46.597 −32.191 1.00 18.93 BBBB ATOM 3383 CB MET B 103 3.928 −45.477 −31.781 1.00 20.02 BBBB ATOM 3384 CG MET B 103 3.121 −44.888 −32.944 1.00 21.61 BBBB ATOM 3385 SD MET B 103 4.212 −44.135 −34.157 1.00 23.45 BBBB ATOM 3386 CE MET B 103 4.718 −42.680 −33.271 1.00 21.40 BBBB ATOM 3387 C MET B 103 5.612 −47.128 −30.957 1.00 18.98 BBBB ATOM 3388 O MET B 103 6.134 −46.357 −30.158 1.00 17.96 BBBB ATOM 3389 N GLY B 104 5.640 −48.450 −30.827 1.00 21.56 BBBB ATOM 3390 CA GLY B 104 6.275 −49.080 −29.686 1.00 21.89 BBBB ATOM 3391 C GLY B 104 5.192 −49.614 −28.764 1.00 23.28 BBBB ATOM 3392 O GLY B 104 4.009 −49.353 −28.980 1.00 22.50 BBBB ATOM 3393 N GLY B 105 5.583 −50.364 −27.741 1.00 23.01 BBBB ATOM 3394 CA GLY B 105 4.593 −50.905 −26.827 1.00 23.54 BBBB ATOM 3395 C GLY B 105 4.358 −52.380 −27.078 1.00 23.17 BBBB ATOM 3396 O GLY B 105 4.449 −52.844 −28.214 1.00 22.69 BBBB ATOM 3397 N TYR B 106 4.018 −53.118 −26.026 1.00 22.87 BBBB ATOM 3398 CA TYR B 106 3.818 −54.554 −26.159 1.00 22.37 BBBB ATOM 3399 CB TYR B 106 3.632 −55.181 −24.774 1.00 25.08 BBBB ATOM 3400 CG TYR B 106 4.864 −55.008 −23.929 1.00 28.19 BBBB ATOM 3401 CD1 TYR B 106 4.869 −54.153 −22.830 1.00 31.96 BBBB ATOM 3402 CE1 TYR B 106 6.043 −53.915 −22.108 1.00 33.13 BBBB ATOM 3403 CD2 TYR B 106 6.058 −55.631 −24.282 1.00 31.27 BBBB ATOM 3404 CE2 TYR B 106 7.234 −55.400 −23.569 1.00 32.27 BBBB ATOM 3405 CZ TYR B 106 7.219 −54.541 −22.487 1.00 33.19 BBBB ATOM 3406 OH TYR B 106 8.388 −54.291 −21.802 1.00 35.95 BBBB ATOM 3407 C TYR B 106 2.719 −55.018 −27.100 1.00 20.52 BBBB ATOM 3408 O TYR B 106 2.867 −56.052 −27.746 1.00 20.50 BBBB ATOM 3409 N VAL B 107 1.628 −54.270 −27.205 1.00 19.06 BBBB ATOM 3410 CA VAL B 107 0.557 −54.694 −28.099 1.00 18.06 BBBB ATOM 3411 CB VAL B 107 −0.690 −53.774 −27.978 1.00 20.95 BBBB ATOM 3412 CG1 VAL B 107 −0.407 −52.407 −28.589 1.00 21.39 BBBB ATOM 3413 CG2 VAL B 107 −1.879 −54.433 −28.658 1.00 21.30 BBBB ATOM 3414 C VAL B 107 1.015 −54.743 −29.559 1.00 17.45 BBBB ATOM 3415 O VAL B 107 0.502 −55.536 −30.346 1.00 16.99 BBBB ATOM 3416 N SER B 108 1.991 −53.916 −29.918 1.00 17.96 BBBB ATOM 3417 CA SER B 108 2.488 −53.892 −31.290 1.00 19.67 BBBB ATOM 3418 CB SER B 108 3.424 −52.691 −31.508 1.00 19.56 BBBB ATOM 3419 OG SER B 108 4.666 −52.824 −30.837 1.00 19.63 BBBB ATOM 3420 C SER B 108 3.197 −55.187 −31.694 1.00 20.38 BBBB ATOM 3421 O SER B 108 3.385 −55.449 −32.884 1.00 21.25 BBBB ATOM 3422 N GLY B 109 3.595 −55.995 −30.710 1.00 19.59 BBBB ATOM 3423 CA GLY B 109 4.251 −57.256 −31.023 1.00 20.03 BBBB ATOM 3424 C GLY B 109 3.311 −58.170 −31.792 1.00 19.61 BBBB ATOM 3425 O GLY B 109 3.579 −58.517 −32.940 1.00 19.24 BBBB ATOM 3426 N PRO B 110 2.206 −58.606 −31.173 1.00 19.20 BBBB ATOM 3427 CD PRO B 110 1.914 −58.528 −29.729 1.00 19.94 BBBB ATOM 3428 CA PRO B 110 1.251 −59.478 −31.855 1.00 18.99 BBBB ATOM 3429 CB PRO B 110 0.198 −59.737 −30.778 1.00 20.41 BBBB ATOM 3430 CG PRO B 110 0.998 −59.720 −29.515 1.00 19.81 BBBB ATOM 3431 C PRO B 110 0.651 −58.761 −33.075 1.00 19.22 BBBB ATOM 3432 O PRO B 110 0.406 −59.371 −34.116 1.00 17.13 BBBB ATOM 3433 N GLY B 111 0.407 −57.462 −32.927 1.00 19.03 BBBB ATOM 3434 CA GLY B 111 −0.160 −56.702 −34.025 1.00 19.60 BBBB ATOM 3435 C GLY B 111 0.764 −56.714 −35.226 1.00 19.59 BBBB ATOM 3436 O GLY B 111 0.330 −56.979 −36.339 1.00 21.10 BBBB ATOM 3437 N GLY B 112 2.043 −56.429 −34.995 1.00 19.78 BBBB ATOM 3438 CA GLY B 112 3.014 −56.417 −36.074 1.00 19.97 BBBB ATOM 3439 C GLY B 112 3.147 −57.783 −36.724 1.00 20.43 BBBB ATOM 3440 O GLY B 112 3.233 −57.896 −37.949 1.00 19.94 BBBB ATOM 3441 N LEU B 113 3.167 −58.828 −35.903 1.00 19.26 BBBB ATOM 3442 CA LEU B 113 3.265 −60.184 −36.429 1.00 19.49 BBBB ATOM 3443 CB LEU B 113 3.405 −61.198 −35.289 1.00 18.38 BBBB ATOM 3444 CG LEU B 113 4.777 −61.270 −34.605 1.00 20.59 BBBB ATOM 3445 CD1 LEU B 113 4.656 −62.059 −33.311 1.00 20.01 BBBB ATOM 3446 CD2 LEU B 113 5.794 −61.914 −35.538 1.00 20.23 BBBB ATOM 3447 C LEU B 113 2.040 −60.521 −37.274 1.00 18.73 BBBB ATOM 3448 O LEU B 113 2.143 −61.252 −38.255 1.00 18.44 BBBB ATOM 3449 N ALA B 114 0.875 −60.010 −36.892 1.00 18.96 BBBB ATOM 3450 CA ALA B 114 −0.334 −60.292 −37.661 1.00 18.70 BBBB ATOM 3451 CB ALA B 114 −1.562 −59.855 −36.889 1.00 16.45 BBBB ATOM 3452 C ALA B 114 −0.288 −59.578 −39.019 1.00 19.30 BBBB ATOM 3453 O ALA B 114 −0.602 −60.167 −40.052 1.00 20.62 BBBB ATOM 3454 N ALA B 115 0.082 −58.303 −39.000 1.00 20.57 BBBB ATOM 3455 CA ALA B 115 0.167 −57.516 −40.229 1.00 21.84 BBBB ATOM 3456 CB ALA B 115 0.636 −56.108 −39.911 1.00 19.85 BBBB ATOM 3457 C ALA B 115 1.140 −58.192 −41.189 1.00 21.58 BBBB ATOM 3458 O ALA B 115 0.815 −58.464 −42.345 1.00 22.14 BBBB ATOM 3459 N TRP B 116 2.334 −58.476 −40.688 1.00 22.12 BBBB ATOM 3460 CA TRP B 116 3.365 −59.126 −41.478 1.00 23.22 BBBB ATOM 3461 CB TRP B 116 4.584 −59.367 −40.579 1.00 26.08 BBBB ATOM 3462 CG TRP B 116 5.699 −60.136 −41.204 1.00 27.40 BBBB ATOM 3463 CD2 TRP B 116 6.168 −61.418 −40.793 1.00 28.77 BBBB ATOM 3464 CE2 TRP B 116 7.234 −61.771 −41.655 1.00 30.37 BBBB ATOM 3465 CE3 TRP B 116 5.794 −62.308 −39.778 1.00 30.49 BBBB ATOM 3466 CD1 TRP B 116 6.473 −59.761 −42.271 1.00 28.30 BBBB ATOM 3467 NE1 TRP B 116 7.401 −60.742 −42.547 1.00 29.04 BBBB ATOM 3468 CZ2 TRP B 116 7.929 −62.981 −41.529 1.00 31.08 BBBB ATOM 3469 CZ3 TRP B 116 6.485 −63.510 −39.653 1.00 31.85 BBBB ATOM 3470 CH2 TRP B 116 7.541 −63.834 −40.527 1.00 32.27 BBBB ATOM 3471 C TRP B 116 2.871 −60.434 −42.123 1.00 23.55 BBBB ATOM 3472 O TRP B 116 3.048 −60.643 −43.329 1.00 22.19 BBBB ATOM 3473 N SER B 117 2.231 −61.304 −41.338 1.00 21.35 BBBB ATOM 3474 CA SER B 117 1.735 −62.573 −41.873 1.00 22.61 BBBB ATOM 3475 CB SER B 117 1.167 −63.462 −40.756 1.00 20.72 BBBB ATOM 3476 OG SER B 117 0.010 −62.889 −40.169 1.00 22.72 BBBB ATOM 3477 C SER B 117 0.665 −62.383 −42.940 1.00 23.56 BBBB ATOM 3478 O SER B 117 0.463 −63.262 −43.780 1.00 23.11 BBBB ATOM 3479 N LEU B 118 −0.020 −61.242 −42.905 1.00 24.40 BBBB ATOM 3480 CA LEU B 118 −1.069 −60.957 −43.882 1.00 25.70 BBBB ATOM 3481 CB LEU B 118 −2.195 −60.155 −43.227 1.00 25.80 BBBB ATOM 3482 CG LEU B 118 −3.012 −60.889 −42.159 1.00 26.56 BBBB ATOM 3483 CD1 LEU B 118 −3.905 −59.895 −41.433 1.00 26.62 BBBB ATOM 3484 CD2 LEU B 118 −3.841 −62.000 −42.801 1.00 26.51 BBBB ATOM 3485 C LEU B 118 −0.539 −60.193 −45.094 1.00 26.87 BBBB ATOM 3486 O LEU B 118 −1.292 −59.878 −46.021 1.00 26.69 BBBB ATOM 3487 N GLY B 119 0.755 −59.898 −45.085 1.00 26.39 BBBB ATOM 3488 CA GLY B 119 1.354 −59.174 −46.192 1.00 27.80 BBBB ATOM 3489 C GLY B 119 1.142 −57.671 −46.120 1.00 27.64 BBBB ATOM 3490 O GLY B 119 1.293 −56.972 −47.122 1.00 28.49 BBBB ATOM 3491 N ILE B 120 0.786 −57.173 −44.940 1.00 25.88 BBBB ATOM 3492 CA ILE B 120 0.568 −55.744 −44.731 1.00 24.85 BBBB ATOM 3493 CB ILE B 120 −0.507 −55.497 −43.652 1.00 24.64 BBBB ATOM 3494 CG2 ILE B 120 −0.648 −54.000 −43.397 1.00 24.49 BBBB ATOM 3495 CG1 ILE B 120 −1.839 −56.112 −44.093 1.00 24.61 BBBB ATOM 3496 CD1 ILE B 120 −2.891 −56.170 −42.991 1.00 23.34 BBBB ATOM 3497 C ILE B 120 1.879 −55.121 −44.272 1.00 24.55 BBBB ATOM 3498 O ILE B 120 2.465 −55.551 −43.275 1.00 23.69 BBBB ATOM 3499 N PRO B 121 2.365 −54.098 −44.995 1.00 23.85 BBBB ATOM 3500 CD PRO B 121 1.780 −53.400 −46.154 1.00 23.64 BBBB ATOM 3501 CA PRO B 121 3.625 −53.477 −44.591 1.00 22.63 BBBB ATOM 3502 CB PRO B 121 3.872 −52.440 −45.691 1.00 23.83 BBBB ATOM 3503 CG PRO B 121 2.485 −52.053 −46.102 1.00 23.96 BBBB ATOM 3504 C PRO B 121 3.583 −52.869 −43.196 1.00 22.21 BBBB ATOM 3505 O PRO B 121 2.617 −52.208 −42.810 1.00 22.46 BBBB ATOM 3506 N VAL B 122 4.641 −53.114 −42.437 1.00 21.69 BBBB ATOM 3507 CA VAL B 122 4.743 −52.594 −41.083 1.00 22.03 BBBB ATOM 3508 CB VAL B 122 5.184 −53.694 −40.095 1.00 21.80 BBBB ATOM 3509 CG1 VAL B 122 5.426 −53.085 −38.724 1.00 21.97 BBBB ATOM 3510 CG2 VAL B 122 4.133 −54.789 −40.035 1.00 22.19 BBBB ATOM 3511 C VAL B 122 5.754 −51.465 −41.021 1.00 21.29 BBBB ATOM 3512 O VAL B 122 6.892 −51.605 −41.479 1.00 22.83 BBBB ATOM 3513 N VAL B 123 5.330 −50.338 −40.464 1.00 20.94 BBBB ATOM 3514 CA VAL B 123 6.200 −49.184 −40.310 1.00 20.82 BBBB ATOM 3515 CB VAL B 123 5.580 −47.902 −40.932 1.00 22.16 BBBB ATOM 3516 CG1 VAL B 123 6.516 −46.722 −40.709 1.00 20.83 BBBB ATOM 3517 CG2 VAL B 123 5.322 −48.111 −42.420 1.00 22.66 BBBB ATOM 3518 C VAL B 123 6.338 −48.953 −38.812 1.00 21.09 BBBB ATOM 3519 O VAL B 123 5.341 −48.986 −38.093 1.00 21.48 BBBB ATOM 3520 N LEU B 124 7.557 −48.720 −38.340 1.00 20.53 BBBB ATOM 3521 CA LEU B 124 7.749 −48.485 −36.915 1.00 22.10 BBBB ATOM 3522 CB LEU B 124 8.578 −49.606 −36.286 1.00 22.00 BBBB ATOM 3523 CG LEU B 124 8.160 −51.051 −36.551 1.00 22.45 BBBB ATOM 3524 CD1 LEU B 124 9.196 −51.974 −35.905 1.00 23.90 BBBB ATOM 3525 CD2 LEU B 124 6.765 −51.313 −36.003 1.00 22.34 BBBB ATOM 3526 C LEU B 124 8.452 −47.172 −36.633 1.00 22.36 BBBB ATOM 3527 O LEU B 124 9.218 −46.660 −37.461 1.00 20.75 BBBB ATOM 3528 N HIS B 125 8.182 −46.638 −35.447 1.00 21.40 BBBB ATOM 3529 CA HIS B 125 8.814 −45.413 −34.981 1.00 21.42 BBBB ATOM 3530 CB HIS B 125 7.858 −44.218 −35.067 1.00 21.57 BBBB ATOM 3531 CG HIS B 125 8.432 −42.948 −34.511 1.00 23.73 BBBB ATOM 3532 CD2 HIS B 125 8.300 −42.368 −33.295 1.00 22.15 BBBB ATOM 3533 ND1 HIS B 125 9.274 −42.127 −35.236 1.00 26.23 BBBB ATOM 3534 CE1 HIS B 125 9.631 −41.095 −34.490 1.00 24.20 BBBB ATOM 3535 NE2 HIS B 125 9.054 −41.218 −33.307 1.00 26.07 BBBB ATOM 3536 C HIS B 125 9.196 −45.642 −33.519 1.00 21.70 BBBB ATOM 3537 O HIS B 125 8.378 −46.117 −32.725 1.00 19.81 BBBB ATOM 3538 N GLU B 126 10.444 −45.332 −33.286 1.00 21.20 BBBB ATOM 3539 CA GLU B 126 10.947 −45.452 −31.817 1.00 22.15 BBBB ATOM 3540 CB GLU B 126 12.252 −46.246 −31.790 1.00 21.99 BBBB ATOM 3541 CG GLU B 126 12.958 −46.206 −30.439 1.00 22.04 BBBB ATOM 3542 CD GLU B 126 12.119 −46.824 −29.338 1.00 21.43 BBBB ATOM 3543 OE1 GLU B 126 11.767 −48.014 −29.471 1.00 21.92 BBBB ATOM 3544 OE2 GLU B 126 11.807 −46.124 −28.349 1.00 21.08 BBBB ATOM 3545 C GLU B 126 11.205 −44.027 −31.326 1.00 21.93 BBBB ATOM 3546 O GLU B 126 12.016 −43.300 −31.908 1.00 21.33 BBBB ATOM 3547 N GLN B 127 10.520 −43.624 −30.259 1.00 22.62 BBBB ATOM 3548 CA GLN B 127 10.682 −42.270 −29.735 1.00 22.81 BBBB ATOM 3549 CB GLN B 127 9.414 −41.814 −28.989 1.00 23.56 BBBB ATOM 3550 CG GLN B 127 8.147 −41.783 −29.830 1.00 24.46 BBBB ATOM 3551 CD GLN B 127 7.312 −43.041 −29.687 1.00 25.85 BBBB ATOM 3552 OE1 GLN B 127 6.842 −43.366 −28.591 1.00 23.78 BBBB ATOM 3553 NE2 GLN B 127 7.119 −43.758 −30.797 1.00 24.91 BBBB ATOM 3554 C GLN B 127 11.874 −42.087 −28.809 1.00 22.39 BBBB ATOM 3555 O GLN B 127 12.399 −40.976 −28.682 1.00 22.43 BBBB ATOM 3556 N ASN B 128 12.314 −43.173 −28.177 1.00 22.35 BBBB ATOM 3557 CA ASN B 128 13.406 −43.097 −27.216 1.00 22.96 BBBB ATOM 3558 CB ASN B 128 13.136 −44.080 −26.064 1.00 22.85 BBBB ATOM 3559 CG ASN B 128 11.742 −43.919 −25.474 1.00 23.25 BBBB ATOM 3560 OD1 ASN B 128 10.804 −44.632 −25.848 1.00 26.04 BBBB ATOM 3561 ND2 ASN B 128 11.597 −42.975 −24.556 1.00 22.68 BBBB ATOM 3562 C ASN B 128 14.824 −43.314 −27.742 1.00 23.87 BBBB ATOM 3563 O ASN B 128 15.026 −43.856 −28.830 1.00 24.05 BBBB ATOM 3564 N GLY B 129 15.798 −42.885 −26.940 1.00 24.35 BBBB ATOM 3565 CA GLY B 129 17.203 −43.019 −27.294 1.00 25.36 BBBB ATOM 3566 C GLY B 129 17.642 −44.468 −27.280 1.00 25.97 BBBB ATOM 3567 O GLY B 129 18.643 −44.836 −27.891 1.00 25.48 BBBB ATOM 3568 N ILE B 130 16.886 −45.290 −26.565 1.00 26.18 BBBB ATOM 3569 CA ILE B 130 17.160 −46.716 −26.488 1.00 28.00 BBBB ATOM 3570 CB ILE B 130 17.480 −47.145 −25.033 1.00 28.45 BBBB ATOM 3571 CG2 ILE B 130 16.323 −46.785 −24.102 1.00 28.52 BBBB ATOM 3572 CG1 ILE B 130 17.776 −48.642 −24.986 1.00 29.33 BBBB ATOM 3673 CD1 ILE B 130 18.097 −49.149 −23.593 1.00 31.39 BBBB ATOM 3574 C ILE B 130 15.909 −47.435 −26.999 1.00 27.44 BBBB ATOM 3575 O ILE B 130 14.793 −47.103 −26.610 1.00 28.58 BBBB ATOM 3576 N ALA B 131 16.097 −48.405 −27.887 1.00 26.98 BBBB ATOM 3577 CA ALA B 131 14.978 −49.139 −28.461 1.00 25.88 BBBB ATOM 3578 CB ALA B 131 15.485 −50.102 −29.525 1.00 25.02 BBBB ATOM 3579 C ALA B 131 14.171 −49.901 −27.413 1.00 25.20 BBBB ATOM 3580 O ALA B 131 14.732 −50.544 −26.533 1.00 25.01 BBBB ATOM 3581 N GLY B 132 12.851 −49.814 −27.506 1.00 24.52 BBBB ATOM 3582 CA GLY B 132 12.007 −50.532 −26.568 1.00 24.05 BBBB ATOM 3583 C GLY B 132 12.150 −52.019 −26.831 1.00 23.35 BBBB ATOM 3584 O GLY B 132 12.582 −52.419 −27.904 1.00 22.89 BBBB ATOM 3585 N LEU B 133 11.788 −52.846 −25.860 1.00 23.38 BBBB ATOM 3586 CA LEU B 133 11.903 −54.293 −26.020 1.00 24.54 BBBB ATOM 3587 CB LEU B 133 11.328 −54.996 −24.786 1.00 25.48 BBBB ATOM 3588 CG LEU B 133 11.388 −56.527 −24.780 1.00 27.50 BBBB ATOM 3589 CD1 LEU B 133 12.840 −56.984 −24.866 1.00 28.69 BBBB ATOM 3590 CD2 LEU B 133 10.735 −57.059 −23.509 1.00 28.04 BBBB ATOM 3591 C LEU B 133 11.209 −54.833 −27.276 1.00 22.84 BBBB ATOM 3592 O LEU B 133 11.784 −55.019 −28.027 1.00 21.86 BBBB ATOM 3593 N THR B 134 9.975 −54.401 −27.499 1.00 21.72 BBBB ATOM 3594 CA THR B 134 9.202 −54.860 −28.639 1.00 21.22 BBBB ATOM 3595 CB THR B 134 7.716 −54.509 −28.449 1.00 20.99 BBBB ATOM 3596 OG1 THR B 134 7.257 −55.075 −27.210 1.00 20.94 BBBB ATOM 3597 CG2 THR B 134 6.872 −55.073 −29.600 1.00 20.64 BBBB ATOM 3598 C THR B 134 9.693 −54.326 −29.986 1.00 20.62 BBBB ATOM 3599 O THR B 134 9.843 −55.091 −30.932 1.00 20.33 BBBB ATOM 3600 N ASN B 135 9.932 −53.021 −30.075 1.00 21.24 BBBB ATOM 3601 CA ASN B 135 10.407 −52.419 −31.324 1.00 20.50 BBBB ATOM 3602 CB ASN B 135 10.637 −50.911 −31.142 1.00 19.58 BBBB ATOM 3603 CG ASN B 135 9.457 −50.058 −31.597 1.00 19.93 BBBB ATOM 3604 OD1 ASN B 135 9.454 −48.837 −31.390 1.00 21.78 BBBB ATOM 3605 ND2 ASN B 135 8.467 −50.677 −32.219 1.00 17.21 BBBB ATOM 3606 C ASN B 135 11.724 −53.064 −31.767 1.00 20.78 BBBB ATOM 3607 O ASN B 135 11.945 −53.290 −32.953 1.00 20.41 BBBB ATOM 3608 N LYS B 136 12.595 −53.366 −30.809 1.00 21.46 BBBB ATOM 3609 CA LYS B 136 13.886 −53.949 −31.144 1.00 22.79 BBBB ATOM 3610 CB LYS B 136 14.713 −54.196 −29.879 1.00 24.70 BBBB ATOM 3611 CG LYS B 136 16.183 −54.424 −30.178 1.00 27.75 BBBB ATOM 3612 CD LYS B 136 16.998 −54.494 −28.902 1.00 30.17 BBBB ATOM 3613 CE LYS B 136 18.479 −54.671 −29.203 1.00 32.33 BBBB ATOM 3614 NZ LYS B 136 19.278 −54.641 −27.944 1.00 33.37 BBBB ATOM 3615 C LYS B 136 13.793 −55.229 −31.966 1.00 23.46 BBBB ATOM 3616 O LYS B 136 14.561 −55.407 −32.912 1.00 23.71 BBBB ATOM 3617 N TRP B 137 12.868 −56.127 −31.633 1.00 21.78 BBBB ATOM 3618 CA TRP B 137 12.753 −57.345 −32.424 1.00 22.06 BBBB ATOM 3619 CB TRP B 137 12.361 −58.552 −31.553 1.00 21.20 BBBB ATOM 3620 CG TRP B 137 10.990 −58.525 −30.922 1.00 20.23 BBBB ATOM 3621 CD2 TRP B 137 9.748 −58.877 −31.544 1.00 18.68 BBBB ATOM 3622 CE2 TRP B 137 8.743 −58.780 −30.555 1.00 18.97 BBBB ATOM 3623 CE3 TRP B 137 9.383 −59.270 −32.840 1.00 19.75 BBBB ATOM 3624 CD1 TRP B 137 10.696 −58.231 −29.618 1.00 19.62 BBBB ATOM 3625 NE1 TRP B 137 9.349 −58.385 −29.390 1.00 19.31 BBBB ATOM 3626 CZ2 TRP B 137 7.401 −59.058 −30.821 1.00 18.18 BBBB ATOM 3627 CZ3 TRP B 137 8.046 −59.549 −33.107 1.00 18.87 BBBB ATOM 3628 CH2 TRP B 137 7.072 −59.440 −32.099 1.00 18.94 BBBB ATOM 3629 C TRP B 137 11.768 −57.202 −33.574 1.00 21.75 BBBB ATOM 3630 O TRP B 137 11.936 −57.822 −34.623 1.00 21.76 BBBB ATOM 3631 N LEU B 138 10.741 −56.381 −33.386 1.00 21.61 BBBB ATOM 3632 CA LEU B 138 9.744 −56.188 −34.431 1.00 23.15 BBBB ATOM 3633 CB LEU B 138 8.618 −55.305 −33.886 1.00 23.87 BBBB ATOM 3634 CG LEU B 138 7.312 −55.155 −34.664 1.00 26.48 BBBB ATOM 3635 CD1 LEU B 138 6.672 −56.508 −34.915 1.00 25.34 BBBB ATOM 3636 CD2 LEU B 138 6.383 −54.267 −33.851 1.00 25.90 BBBB ATOM 3637 C LEU B 138 10.384 −55.558 −35.676 1.00 23.07 BBBB ATOM 3638 O LEU B 138 9.958 −55.801 −36.809 1.00 22.68 BBBB ATOM 3639 N ALA B 139 11.423 −54.763 −35.453 1.00 23.34 BBBB ATOM 3640 CA ALA B 139 12.128 −54.092 −36.542 1.00 25.29 BBBB ATOM 3641 CB ALA B 139 13.298 −53.287 −35.984 1.00 24.97 BBBB ATOM 3642 C ALA B 139 12.624 −55.064 −37.610 1.00 26.83 BBBB ATOM 3643 O ALA B 139 12.829 −54.672 −38.754 1.00 27.29 BBBB ATOM 3644 N LYS B 140 12.801 −56.332 −37.241 1.00 27.38 BBBB ATOM 3645 CA LYS B 140 13.279 −57.337 −38.182 1.00 28.05 BBBB ATOM 3646 CB LYS B 140 13.893 −58.501 −37.401 1.00 29.91 BBBB ATOM 3647 CG LYS B 140 15.134 −58.057 −36.635 1.00 31.62 BBBB ATOM 3648 CD LYS B 140 15.719 −59.149 −35.757 1.00 33.53 BBBB ATOM 3649 CE LYS B 140 16.974 −58.634 −35.055 1.00 34.46 BBBB ATOM 3650 NZ LYS B 140 17.692 −59.713 −34.320 1.00 36.17 BBBB ATOM 3651 C. LYS B 140 12.254 −57.833 −39.212 1.00 27.83 BBBB ATOM 3652 O LYS B 140 12.602 −58.562 −40.142 1.00 27.80 BBBB ATOM 3653 N ILE B 141 10.992 −57.445 −39.052 1.00 26.40 BBBB ATOM 3654 CA ILE B 141 9.963 −57.818 −40.016 1.00 26.09 BBBB ATOM 3655 CB ILE B 141 8.854 −58.721 −39.405 1.00 26.39 BBBB ATOM 3656 CG2 ILE B 141 9.401 −60.118 −39.145 1.00 28.33 BBBB ATOM 3657 CG1 ILE B 141 8.298 −58.092 −38.127 1.00 26.45 BBBB ATOM 3658 CD1 ILE B 141 7.136 −58.845 −37.549 1.00 26.95 BBBB ATOM 3659 C ILE B 141 9.316 −56.542 −40.530 1.00 25.81 BBBB ATOM 3660 O ILE B 141 8.353 −56.586 −41.305 1.00 26.10 BBBB ATOM 3661 N ALA B 142 9.856 −55.405 −40.097 1.00 23.78 BBBB ATOM 3662 CA ALA B 142 9.331 −54.107 −40.498 1.00 25.03 BBBB ATOM 3663 CB ALA B 142 9.717 −53.046 −39.466 1.00 24.89 BBBB ATOM 3664 C ALA B 142 9.816 −53.680 −41.880 1.00 25.08 BBBB ATOM 3665 O ALA B 142 10.973 −53.894 −42.237 1.00 24.93 BBBB ATOM 3666 N THR B 143 8.920 −53.075 −42.651 1.00 25.03 BBBB ATOM 3667 CA THR B 143 9.262 −52.595 −43.984 1.00 26.10 BBBB ATOM 3668 CB THR B 143 7.987 −52.318 −44.816 1.00 25.75 BBBB ATOM 3669 OG1 THR B 143 7.249 −53.534 −44.970 1.00 25.54 BBBB ATOM 3670 CG2 THR B 143 8.345 −51.782 −46.207 1.00 26.92 BBBB ATOM 3671 C THE B 143 10.079 −51.310 −43.863 1.00 26.63 BBBB ATOM 3672 O THR B 143 10.996 −51.061 −44.656 1.00 27.13 BBBB ATOM 3673 N LYS B 144 9.753 −50.506 −42.853 1.00 24.95 BBBB ATOM 3674 CA LYS B 144 10.436 −49.238 −42.618 1.00 24.73 BBBB ATOM 3675 CB LYS B 144 9.688 −48.103 −43.329 1.00 26.20 BBBB ATOM 3676 CG LYS B 144 10.202 −46.710 −43.013 1.00 27.44 BBBB ATOM 3677 CO LYS B 144 11.602 −46.480 −43.558 1.00 29.01 BBBB ATOM 3678 CE. LYS B 144 12.055 −45.051 −43.293 1.00 29.74 BBBB ATOM 3679 NZ LYS B 144 13.406 −44.774 −43.854 1.00 31.29 BBBB ATOM 3680 C LYS B 144 10.506 −48.943 −41.125 1.00 24.61 BBBB ATOM 3681 O LYS B 144 9.493 −49.008 −40.423 1.00 23.36 BBBB ATOM 3682 N VAL B 145 11.707 −48.623 −40.656 1.00 23.68 BBBB ATOM 3683 CA VAL B 145 11.947 −48.311 −39.252 1.00 23.62 BBBB ATOM 3684 CB VAL B 145 12.981 −49.279 −38.617 1.00 23.66 BBBB ATOM 3685 CG1 VAL B 145 13.083 −49.014 −37.114 1.00 24.44 BBBB ATOM 3686 CG2 VAL B 145 12.589 −50.724 −38.878 1.00 23.51 BBBB ATOM 3687 C VAL B 145 12.510 −46.900 −39.125 1.00 24.09 BBBB ATOM 3688 O VAL B 145 13.473 −46.545 −39.808 1.00 23.68 BBBB ATOM 3689 N MET B 146 11.902 −46.103 −38.251 1.00 23.84 BBBB ATOM 3690 CA MET B 146 12.338 −44.736 −37.993 1.00 23.15 BBBB ATOM 3691 CB MET B 146 11.274 −43.729 −38.448 1.00 24.72 BBBB ATOM 3692 CG MET B 146 11.130 −43.577 −39.970 1.00 21.76 BBBB ATOM 3693 SD MET B 146 9.649 −42.636 −40.468 1.00 25.05 BBBB ATOM 3694 CE MET B 146 8.376 −43.846 −40.325 1.00 21.96 BBBB ATOM 3695 C MET B 146 12.567 −44.593 −36.488 1.00 24.69 BBBB ATOM 3696 O MET B 146 11.963 −45.311 −35.689 1.00 22.43 BBBB ATOM 3697 N GLN B 147 13.456 −43.678 −36.112 1.00 23.37 BBBB ATOM 3698 CA GLN B 147 13.762 −43.418 −34.712 1.00 25.05 BBBB ATOM 3699 CB GLN B 147 15.067 −44.114 +34.301 1.00 24.99 BBBB ATOM 3700 CG GLN B 147 16.259 −43.750 −35.169 1.00 26.10 BBBB ATOM 3701 CD GLN B 147 17.527 −44.508 −34.803 1.00 26.65 BBBB ATOM 3702 OE1 GLN B 147 18.425 −44.671 −35.637 1.00 28.62 BBBB ATOM 3703 NE2 GLN B 147 17.615 −44.966 −33.558 1.00 26.05 BBBB ATOM 3704 C GLN B 147 13.880 −41.911 −34.515 1.00 26.28 BBBB ATOM 3705 O GLN B 147 14.292 −41.177 −35.430 1.00 25.02 BBBB ATOM 3706 N ALA B 148 13.518 −41.452 −33.323 1.00 26.58 BBBB ATOM 3707 CA ALA B 148 13.559 −40.032 −33.009 1.00 26.88 BBBB ATOM 3708 CB ALA B 148 12.853 −39.776 −31.685 1.00 26.71 BBBB ATOM 3709 C ALA B 148 14.983 −39.502 −32.954 1.00 27.88 BBBB ATOM 3710 O ALA B 148 15.293 −38.463 −33.545 1.00 27.38 BBBB ATOM 3711 N PHE B 149 15.847 −40.219 −32.242 1.00 27.92 BBBB ATOM 3712 CA PHE B 149 17.239 −39.820 −32.098 1.00 29.39 BBBB ATOM 3713 CB PHE B 149 17.596 −39.631 −30.617 1.00 28.95 BBBB ATOM 3714 CG PHE B 149 16.549 −38.910 −29.821 1.00 28.91 BBBB ATOM 3715 CD1 PHE B 149 15.745 −39.603 −28.929 1.00 27.96 BBBB ATOM 3716 CD2 PHE B 149 16.372 −37.537 −29.957 1.00 29.03 BBBB ATOM 3717 CE1 PHE B 149 14.779 −38.945 −28.178 1.00 28.64 BBBB ATOM 3718 CE2 PHE B 149 15.406 −36.866 −29.211 1.00 30.10 BBBB ATOM 3719 CZ PHE B 149 14.608 −37.575 −28.317 1.00 29.02 BBBB ATOM 3720 C PHE B 149 18.153 −40.893 −32.673 1.00 30.03 BBBB ATOM 3721 O PHE B 149 17.750 −42.036 −32.849 1.00 30.05 BBBB ATOM 3722 N PRO B 150 19.401 −40.530 −32.991 1.00 31.73 BBBB ATOM 3723 CD PRO B 150 20.018 −39.192 −33.018 1.00 32.39 BBBB ATOM 3724 CA PRO B 150 20.310 −41.541 −33.535 1.00 31.87 BBBB ATOM 3725 CB PRO B 150 21.418 −40.698 −34.154 1.00 33.07 BBBB ATOM 3726 CG PRO B 150 21.480 −39.517 −33.238 1.00 33.70 BBBB ATOM 3727 C PRO B 150 20.809 −42.411 −32.376 1.00 31.93 BBBB ATOM 3728 O PRO B 150 20.873 −41.945 −31.239 1.00 31.39 BBBB ATOM 3729 N GLY B 151 21.130 −43.671 −32.651 1.00 31.67 BBBB ATOM 3730 CA GLY B 151 21.629 −44.537 −31.595 1.00 32.62 BBBB ATOM 3731 C GLY B 151 20.717 −45.655 −31.112 1.00 32.88 BBBB ATOM 3732 O GLY B 151 21.206 −46.690 −30.657 1.00 32.98 BBBB ATOM 3733 N ALA B 152 19.403 −45.458 −31.196 1.00 32.24 BBBB ATOM 3734 CA ALA B 152 18.447 −46.476 −30.753 1.00 32.71 BBBB ATOM 3735 CB ALA B 152 17.020 −45.924 −30.817 1.00 31.78 BBBB ATOM 3736 C ALA B 152 18.582 −47.708 −31.643 1.00 33.00 BBBB ATOM 3737 O ALA B 152 18.528 −48.842 −31.169 1.00 32.08 BBBB ATOM 3738 N PHE B 153 18.732 −47.462 −32.941 1.00 33.66 BBBB ATOM 3739 CA PHE B 153 18.925 −48.506 −33.937 1.00 34.83 BBBB ATOM 3740 CB PHE B 153 17.734 −48.611 −34.893 1.00 33.64 BBBB ATOM 3741 CG PHE B 153 16.518 −49.244 −34.289 1.00 32.97 BBBB ATOM 3742 CD1 PHE B 153 15.468 −48.461 −33.823 1.00 31.93 BBBB ATOM 3743 CD2 PHE B 153 16.421 −50.628 −34.184 1.00 32.46 BBBB ATOM 3744 CE1 PHE B 153 14.339 −49.049 −33.265 1.00 32.18 BBBB ATOM 3745 CE2 PHE B 153 15.294 −51.224 −33.626 1.00 31.75 BBBB ATOM 3746 CZ PHE B 153 14.254 −50.435 −33.166 1.00 31.22 BBBB ATOM 3747 C PHE B 153 20.155 −48.075 −34.723 1.00 36.90 BBBB ATOM 3748 O PHE B 153 20.407 −46.878 −34.879 1.00 37.54 BBBB ATOM 3749 N PRO B 154 20.944 −49.040 −35.220 1.00 38.15 BBBB ATOM 3750 CD PRO B 154 20.845 −50.482 −34.932 1.00 38.37 BBBB ATOM 3751 CA PRO B 154 22.158 −48.751 −35.993 1.00 38.97 BBBB ATOM 3752 CB PRO B 154 22.706 −50.143 −36.302 1.00 39.31 BBBB ATOM 3753 CG PRO B 154 22.274 −50.941 −35.108 1.00 39.50 BBBB ATOM 3754 C PRO B 154 21.964 −47.921 −37.266 1.00 39.90 BBBB ATOM 3755 O PRO B 154 22.697 −46.958 −37.496 1.00 39.89 BBBB ATOM 3756 N ASN B 155 20.979 −48.280 −38.088 1.00 40.46 BBBB ATOM 3757 CA ASN B 155 20.765 −47.568 −39.346 1.00 41.08 BBBB ATOM 3758 CB ASN B 155 21.135 −48.488 −40.510 1.00 43.63 BBBB ATOM 3759 CG ASN B 155 22.618 −48.753 −40.585 1.00 45.00 BBBB ATOM 3760 OD1 ASN B 155 23.401 −47.861 −40.922 1.00 46.41 BBBB ATOM 3761 ND2 ASN B 155 23.019 −49.978 −40.259 1.00 45.20 BBBB ATOM 3762 C ASN B 155 19.393 −46.966 −39.627 1.00 40.73 BBBB ATOM 3763 O ASN B 155 19.145 −46.501 −40.742 1.00 41.01 BBBB ATOM 3764 N ALA B 156 18.507 −46.956 −38.638 1.00 38.93 BBBB ATOM 3765 CA ALA B 156 17.170 −46.407 −38.843 1.00 37.55 BBBB ATOM 3766 CB ALA B 156 16.304 −46.689 −37.618 1.00 37.34 BBBB ATOM 3767 C ALA B 156 17.209 −44.909 −39.123 1.00 36.36 BBBB ATOM 3768 O ALA B 156 17.934 −44.171 −38.459 1.00 36.95 BBBB ATOM 3769 N GLU B 157 16.428 −44.464 −40.107 1.00 35.76 BBBB ATOM 3770 CA GLU B 157 16.367 −43.044 −40.460 1.00 34.40 BBBB ATOM 3771 CB GLU B 157 15.375 −42.815 −41.613 1.00 34.84 BBBB ATOM 3772 CG GLU B 157 15.246 −41.349 −42.055 1.00 34.91 BBBB ATOM 3773 CD GLU B 157 14.171 −41.123 −43.117 1.00 36.66 BBBB ATOM 3774 OE1 GLU B 157 13.952 −39.951 −43.509 1.00 37.67 BBBB ATOM 3775 OE2 GLU B 157 13.543 −42.107 −43.563 1.00 35.62 BBBB ATOM 3776 C GLU B 157 15.922 −42.249 −39.231 1.00 33.89 BBBB ATOM 3777 O GLU B 157 14.941 −42.605 −38.574 1.00 33.04 BBBB ATOM 3778 N VAL B 158 16.655 −41.185 −38.915 1.00 32.73 BBBB ATOM 3779 CA VAL B 158 16.337 −40.344 −37.764 1.00 31.16 BBBB ATOM 3780 CB VAL B 158 17.606 −39.680 −37.202 1.00 31.85 BBBB ATOM 3781 CG1 VAL B 158 17.238 −38.729 −36.073 1.00 31.22 BBBB ATOM 3782 CG2 VAL B 158 18.574 −40.752 −36.708 1.00 31.41 BBBB ATOM 3783 C VAL B 158 15.352 −39.260 −38.178 1.00 30.27 BBBB ATOM 3784 O VAL B 158 15.649 −38.445 −39.053 1.00 30.18 BBBB ATOM 3785 N VAL B 159 14.186 −39.241 −37.544 1.00 28.57 BBBB ATOM 3786 CA VAL B 159 13.155 −38.265 −37.889 1.00 28.10 BBBB ATOM 3787 CB VAL B 159 11.942 −38.963 −38.535 1.00 27.81 BBBB ATOM 3788 CG1 VAL B 159 12.365 −39.667 −39.819 1.00 28.61 BBBB ATOM 3789 CG2 VAL B 159 11.336 −39.962 −37.548 1.00 27.61 BBBB ATOM 3790 C VAL B 159 12.636 −37.430 −36.725 1.00 27.64 BBBB ATOM 3791 O VAL B 159 11.757 −36.591 −36.918 1.00 27.97 BBBB ATOM 3792 N GLY B 160 13.168 −37.662 −35.527 1.00 27.60 BBBB ATOM 3793 CA GLY B 160 12.724 −36.921 −34.355 1.00 26.93 BBBB ATOM 3794 C GLY B 160 11.331 −37.312 −33.883 1.00 26.66 BBBB ATOM 3795 O GLY B 160 10.757 −38.275 −34.384 1.00 26.71 BBBB ATOM 3796 N ASN B 161 10.797 −36.569 −32.914 1.00 25.68 BBBB ATOM 3797 CA ASN B 161 9.456 −36.807 −32.375 1.00 25.27 BBBB ATOM 3798 CB ASN B 161 9.481 −36.963 −30.849 1.00 23.89 BBBB ATOM 3799 CG ASN B 161 10.042 −38.285 −30.401 1.00 22.91 BBBB ATOM 3800 OD1 ASN B 161 9.600 −39.335 −30.850 1.00 22.70 BBBB ATOM 3801 ND2 ASN B 161 11.017 −38.243 −29.496 1.00 22.71 BBBB ATOM 3802 C ASN B 161 8.556 −35.618 −32.670 1.00 25.39 BBBB ATOM 3803 O ASN B 161 9.028 −34.499 −32.821 1.00 25.45 BBBB ATOM 3804 N PRO B 162 7.241 −35.849 −32.741 1.00 26.08 BBBB ATOM 3805 CD PRO B 162 6.533 −37.140 −32.710 1.00 25.20 BBBB ATOM 3806 CA PRO B 162 6.315 −34.747 −33.004 1.00 26.14 BBBB ATOM 3807 CB PRO B 162 4.952 −35.431 −32.976 1.00 25.76 BBBB ATOM 3808 CG PRO B 162 5.255 −36.821 −33.430 1.00 26.48 BBBB ATOM 3809 C PRO B 162 6.455 −33.728 −31.866 1.00 27.00 BBBB ATOM 3810 O PRO B 162 6.652 −34.102 −30.703 1.00 25.08 BBBB ATOM 3811 N VAL B 163 6.355 −32.446 −32.203 1.00 27.54 BBBB ATOM 3812 CA VAL B 163 6.456 −31.379 −31.216 1.00 27.75 BBBB ATOM 3813 CB VAL B 163 7.748 −30.561 −31.421 1.00 28.81 BBBB ATOM 3814 CG1 VAL B 163 7.839 −29.451 −30.381 1.00 28.20 BBBB ATOM 3815 CG2 VAL B 163 8.958 −31.471 −31.335 1.00 27.87 BBBB ATOM 3816 C VAL B 163 5.261 −30.440 −31.365 1.00 29.43 BBBB ATOM 3817 O VAL B 163 4.777 −30.227 −32.476 1.00 28.49 BBBB ATOM 3818 N ARG B 164 4.790 −29.891 −30.246 1.00 29.93 BBBB ATOM 3819 CA ARG B 164 3.667 −28.953 −30.246 1.00 32.36 BBBB ATOM 3820 CB ARG B 164 3.430 −28.411 −28.833 1.00 34.56 BBBB ATOM 3821 CG ARG B 164 2.967 −29.439 −27.832 1.00 38.34 BBBB ATOM 3822 CD ARG B 164 3.067 −28.889 −26.417 1.00 41.59 BBBB ATOM 3823 NE ARG B 164 2.481 −27.555 −26.299 1.00 44.08 BBBB ATOM 3824 CZ ARG B 164 2.307 −26.919 −25.144 1.00 45.79 BBBB ATOM 3825 NH1 ARG B 164 2.673 −27.499 −24.008 1.00 46.89 BBBB ATOM 3826 NH2 ARG B 164 1.769 −25.705 −25.123 1.00 47.50 BBBB ATOM 3827 C ARG B 164 3.939 −27.775 −31.187 1.00 31.56 BBBB ATOM 3828 O ARG B 164 5.031 −27.212 −31.191 1.00 30.03 BBBB ATOM 3829 N THR B 165 2.928 −27.401 −31.965 1.00 32.06 BBBB ATOM 3830 CA THR B 165 3.038 −26.307 −32.924 1.00 31.74 BBBB ATOM 3831 CB THR B 165 1.701 −26.104 −33.678 1.00 32.51 BBBB ATOM 3832 OG1 THR B 165 1.198 −27.375 −34.094 1.00 32.54 BBBB ATOM 3833 CG2 THR B 165 1.907 −25.239 −34.916 1.00 32.14 BBBB ATOM 3834 C THR B 165 3.445 −24.976 −32.295 1.00 31.49 BBBB ATOM 3835 O THR B 165 4.236 −24.238 −32.872 1.00 31.48 BBBB ATOM 3836 N ASP B 166 2.907 −24.664 −31.120 1.00 30.86 BBBB ATOM 3837 CA ASP B 166 3.252 −23.404 −30.466 1.00 30.64 BBBB ATOM 3838 CB ASP B 166 2.358 −23.163 −29.242 1.00 33.08 BBBB ATOM 3839 CG ASP B 166 2.185 −24.400 −28.384 1.00 35.24 BBBB ATOM 3840 OD1 ASP B 166 1.315 −24.373 −27.485 1.00 38.19 BBBB ATOM 3841 OD2 ASP B 166 2.908 −25.393 −28.603 1.00 37.17 BBBB ATOM 3842 C ASP B 166 4.729 −23.338 −30.084 1.00 28.64 BBBB ATOM 3843 O ASP B 166 5.321 −22.259 −30.076 1.00 27.92 BBBB ATOM 3844 N VAL B 167 5.328 −24.485 −29.773 1.00 27.08 BBBB ATOM 3845 CA VAL B 167 6.746 −24.503 −29.440 1.00 25.91 BBBB ATOM 3846 CB VAL B 167 7.171 −25.824 −28.757 1.00 25.96 BBBB ATOM 3847 CG1 VAL B 167 8.687 −25.844 −28.586 1.00 24.67 BBBB ATOM 3848 CG2 VAL B 167 6.482 −25.964 −27.396 1.00 26.22 BBBB ATOM 3849 C VAL B 167 7.548 −24.361 −30.736 1.00 25.54 BBBB ATOM 3850 O VAL B 167 8.548 −23.642 −30.787 1.00 25.58 BBBB ATOM 3851 N LEU B 168 7.108 −25.059 −31.778 1.00 26.75 BBBB ATOM 3852 CA LEU B 168 7.780 −25.002 −33.075 1.00 28.46 BBBB ATOM 3853 CB LEU B 168 7.085 −25.930 −34.080 1.00 28.40 BBBB ATOM 3854 CG LEU B 168 7.205 −27.440 −33.890 1.00 28.67 BBBB ATOM 3855 CD1 LEU B 168 6.254 −28.161 −34.854 1.00 30.19 BBBB ATOM 3856 CD2 LEU B 168 8.647 −27.868 −34.129 1.00 28.82 BBBB ATOM 3857 C LEU B 168 7.766 −23.584 −33.632 1.00 29.14 BBBB ATOM 3858 O LEU B 168 8.667 −23.186 −34.369 1.00 29.57 BBBB ATOM 3859 N ALA B 169 6.741 −22.823 −33.267 1.00 30.35 BBBB ATOM 3860 CA ALA B 169 6.580 −21.455 −33.756 1.00 31.43 BBBB ATOM 3861 CB ALA B 169 5.118 −21.030 −33.624 1.00 33.26 BBBB ATOM 3862 C ALA B 169 7.472 −20.427 −33.078 1.00 32.03 BBBB ATOM 3863 O ALA B 169 7.562 −19.284 −33.536 1.00 31.95 BBBB ATOM 3864 N LEU B 170 8.131 −20.824 −31.993 1.00 30.53 BBBB ATOM 3865 CA LEU B 170 9.002 −19.905 −31.268 1.00 29.60 BBBB ATOM 3866 CB LEU B 170 9.601 −20.595 −30.041 1.00 28.66 BBBB ATOM 3867 CG LEU B 170 8.623 −20.954 −28.923 1.00 28.67 BBBB ATOM 3868 CD1 LEU B 170 9.322 −21.845 −27.907 1.00 27.66 BBBB ATOM 3869 CD2 LEU B 170 8.096 −19.675 −28.277 1.00 27.21 BBBB ATOM 3870 C LEU B 170 10.138 −19.363 −32.127 1.00 29.76 BBBB ATOM 3871 O LEU B 170 10.670 −20.064 −32.983 1.00 29.07 BBBB ATOM 3872 N PRO B 171 10.525 −18.099 −31.897 1.00 29.71 BBBB ATOM 3873 CD PRO B 171 9.874 −17.138 −30.989 1.00 30.67 BBBB ATOM 3874 CA PRO B 171 11.611 −17.457 −32.642 1.00 30.11 BBBB ATOM 3875 CB PRO B 171 11.665 −16.054 −32.033 1.00 29.54 BBBB ATOM 3876 CG PRO B 171 10.261 −15.810 −31.605 1.00 30.96 BBBB ATOM 3877 C PRO B 171 12.900 −18.226 −32.374 1.00 30.39 BBBB ATOM 3878 O PRO B 171 12.999 −18.933 −31.363 1.00 30.16 BBBB ATOM 3879 N LEU B 172 13.883 −18.097 −33.263 1.00 28.62 BBBB ATOM 3880 CA LEU B 172 15.157 −18.780 −33.062 1.00 28.33 BBBB ATOM 3881 CB LEU B 172 16.106 −18.557 −34.247 1.00 29.88 BBBB ATOM 3882 CG LEU B 172 15.800 −19.149 −35.628 1.00 32.18 BBBB ATOM 3883 CD1 LEU B 172 15.593 −20.656 −35.510 1.00 32.75 BBBB ATOM 3884 CD2 LEU B 172 14.573 −18.476 −36.222 1.00 33.92 BBBB ATOM 3885 C LEU B 172 15.805 −18.206 −31.805 1.00 26.61 BBBB ATOM 3886 O LEU B 172 15.478 −17.093 −31.388 1.00 26.45 BBBB ATOM 3887 N PRO B 173 16.735 −18.959 −31.190 1.00 25.73 BBBB ATOM 3888 CD PRO B 173 17.093 −20.345 −31.550 1.00 24.63 BBBB ATOM 3889 CA PRO B 173 17.450 −18.550 −29.977 1.00 25.25 BBBB ATOM 3890 CB PRO B 173 18.512 −19.635 −29.827 1.00 25.04 BBBB ATOM 3891 CG PRO B 173 17.818 −20.831 −30.309 1.00 24.90 BBBB ATOM 3892 C PRO B 173 18.066 −17.145 −29.999 1.00 24.24 BBBB ATOM 3893 O PRO B 173 17.791 −16.337 −29.116 1.00 22.89 BBBB ATOM 3894 N GLN B 174 18.899 −16.850 −30.995 1.00 24.48 BBBB ATOM 3895 CA GLN B 174 19.526 −15.527 −31.049 1.00 25.46 BBBB ATOM 3896 CB GLN B 174 20.384 −15.382 −32.313 1.00 26.10 BBBB ATOM 3897 CG GLN B 174 21.173 −14.070 −32.382 1.00 26.21 BBBB ATOM 3898 CD GLN B 174 20.325 −12.883 −32.812 1.00 26.24 BBBB ATOM 3899 OE1 GLN B 174 20.634 −11.732 −32.491 1.00 26.98 BBBB ATOM 3900 NE2 GLN B 174 19.258 −13.154 −33.550 1.00 25.58 BBBB ATOM 3901 C GLN B 174 18.485 −14.408 −30.981 1.00 25.33 BBBB ATOM 3902 O GLN B 174 18.646 −13.432 −30.249 1.00 24.63 BBBB ATOM 3903 N GLN B 175 17.402 −14.555 −31.726 1.00 26.49 BBBB ATOM 3904 CA GLN B 175 16.365 −13.525 −31.718 1.00 28.47 BBBB ATOM 3905 CB GLN B 175 15.333 −13.819 −32.809 1.00 29.48 BBBB ATOM 3906 CG GLN B 175 14.206 −12.805 −32.888 1.00 33.70 BBBB ATOM 3907 CD GLN B 175 13.324 −13.006 −34.109 1.00 35.20 BBBB ATOM 3908 OE1 GLN B 175 12.247 −12.422 −34.215 1.00 38.98 BBBB ATOM 3909 NE2 GLN B 175 13.785 −13.828 −35.042 1.00 37.92 BBBB ATOM 3910 C GLN B 175 15.678 −13.430 −30.355 1.00 27.54 BBBB ATOM 3911 O GLN B 175 15.521 −12.346 −29.796 1.00 26.49 BBBB ATOM 3912 N ARG B 176 15.288 −14.578 −29.818 1.00 28.19 BBBB ATOM 3913 CA ARG B 176 14.611 −14.635 −28.525 1.00 29.01 BBBB ATOM 3914 CB ARG B 176 14.183 −16.088 −28.260 1.00 32.12 BBBB ATOM 3915 CG ARG B 176 13.783 −16.410 −26.825 1.00 34.95 BBBB ATOM 3916 CD ARG B 176 12.879 −17.638 −26.779 1.00 26.93 BBBB ATOM 3917 NE ARG B 176 13.401 −18.749 −27.566 1.00 37.99 BBBB ATOM 3918 CZ ARG B 176 14.458 −19.480 −27.231 1.00 40.44 BBBB ATOM 3919 NH1 ARG B 176 15.121 −19.233 −26.107 1.00 41.22 BBBB ATOM 3920 NH2 ARG B 176 14.866 −20.451 −28.040 1.00 42.79 BBBB ATOM 3921 C ARG B 176 15.449 −14.094 −27.357 1.00 28.58 BBBB ATOM 3922 O ARG B 176 14.933 −13.414 −26.467 1.00 26.70 BBBB ATOM 3923 N LEU B 177 16.744 −14.382 −27.384 1.00 28.60 BBBB ATOM 3924 CA LEU B 177 17.673 −13.970 −26.331 1.00 29.90 BBBB ATOM 3925 CB LEU B 177 18.729 −15.071 −26.140 1.00 30.05 BBBB ATOM 3926 CG LEU B 177 18.323 −16.402 −25.484 1.00 31.35 BBBB ATOM 3927 CD1 LEU B 177 16.893 −16.755 −25.807 1.00 31.63 BBBB ATOM 3928 CD2 LEU B 177 19.266 −17.504 −25.948 1.00 30.16 BBBB ATOM 3929 C LEU B 177 18.384 −12.637 −26.594 1.00 30.48 BBBB ATOM 3930 O LEU B 177 19.148 −12.161 −25.752 1.00 30.67 BBBB ATOM 3931 N ALA B 178 18.128 −12.036 −27.752 1.00 31.18 BBBB ATOM 3932 CA ALA B 178 18.766 −10.776 −28.131 1.00 30.78 BBBB ATOM 3933 CB ALA B 178 18.238 −10.319 −29.496 1.00 32.30 BBBB ATOM 3934 C ALA B 178 18.639 −9.636 −27.123 1.00 31.11 BBBB ATOM 3935 O ALA B 178 17.537 −9.253 −26.726 1.00 30.59 BBBB ATOM 3936 N GLY B 179 19.792 −9.105 −26.718 1.00 30.45 BBBB ATOM 3937 CA GLY B 179 19.846 −7.993 −25.784 1.00 30.10 BBBB ATOM 3938 C GLY B 179 19.392 −8.298 −24.374 1.00 29.54 BBBB ATOM 3939 O GLY B 179 19.288 −7.405 −23.537 1.00 28.79 BBBB ATOM 3940 N ARG B 180 19.129 −9.568 −24.101 1.00 29.31 BBBB ATOM 3941 CA ARG B 180 18.676 −9.965 −22.787 1.00 28.97 BBBB ATOM 3942 CB ARG B 180 18.120 −11.391 −22.868 1.00 28.73 BBBB ATOM 3943 CG ARG B 180 17.281 −11.815 −21.693 1.00 25.80 BBBB ATOM 3944 CD ARG B 180 16.813 −13.245 −21.869 1.00 24.21 BBBB ATOM 3945 NE ARG B 180 15.595 −13.363 −22.665 1.00 23.27 BBBB ATOM 3946 CZ ARG B 180 14.898 −14.489 −22.776 1.00 24.65 BBBB ATOM 3947 NH1 ARG B 180 15.316 −15.579 −22.146 1.00 21.06 BBBB ATOM 3948 NH2 ARG B 180 13.777 −14.529 −23.491 1.00 23.07 BBBB ATOM 3949 C ARG B 180 19.818 −9.874 −21.769 1.00 30.52 BBBB ATOM 3950 O ARG B 180 20.916 −10.398 −21.980 1.00 30.32 BBBB ATOM 3951 N GLU B 181 19.562 −9.171 −20.677 1.00 30.40 BBBB ATOM 3952 CA GLU B 181 20.545 −9.027 −19.621 1.00 31.79 BBBB ATOM 3953 CB GLU B 181 21.157 −7.617 −19.650 1.00 34.59 BBBB ATOM 3954 CG GLU B 181 22.130 −7.422 −20.826 1.00 38.85 BBBB ATOM 3955 CD GLU B 181 22.659 −6.001 −20.957 1.00 41.19 BBBB ATOM 3956 OE1 GLU B 181 23.274 −5.495 −19.996 1.00 43.24 BBBB ATOM 3957 OE2 GLU B 181 22.467 −5.392 −22.032 1.00 43.11 BBBB ATOM 3958 C GLU B 181 19.815 −9.307 −18.313 1.00 31.51 BBBB ATOM 3959 O GLU B 181 18.605 −9.543 −18.313 1.00 33.44 BBBB ATOM 3960 N GLY B 182 20.535 −9.314 −17.203 1.00 29.65 BBBB ATOM 3961 CA GLY B 182 19.871 −9.586 −15.943 1.00 27.75 BBBB ATOM 3962 C GLY B 182 19.989 −11.051 −15.565 1.00 25.32 BBBB ATOM 3963 O GLY B 182 20.573 −11.830 −16.311 1.00 22.00 BBBB ATOM 3964 N PRO B 183 19.414 −11.455 −14.423 1.00 23.79 BBBB ATOM 3965 CD PRO B 183 18.562 −10.609 −13.572 1.00 24.07 BBBB ATOM 3966 CA PRO B 183 19.450 −12.832 −13.913 1.00 22.93 BBBB ATOM 3967 CB PRO B 183 18.480 −12.796 −12.727 1.00 23.23 BBBB ATOM 3968 CG PRO B 183 18.549 −11.381 −12.271 1.00 24.61 BBBB ATOM 3969 C PRO B 183 19.063 −13.912 −14.905 1.00 21.77 BBBB ATOM 3970 O PRO B 183 18.117 −13.758 −15.683 1.00 21.04 BBBB ATOM 3971 N VAL B 184 19.805 −15.011 −14.867 1.00 19.40 BBBB ATOM 3972 CA VAL B 184 19.524 −16.146 −15.729 1.00 18.01 BBBB ATOM 3973 CB VAL B 184 20.597 −17.248 −15.549 1.00 17.45 BBBB ATOM 3974 CG1 VAL B 184 20.171 −18.534 −16.249 1.00 15.59 BBBB ATOM 3975 CG2 VAL B 184 21.931 −16.753 −16.121 1.00 18.46 BBBB ATOM 3976 C VAL B 184 18.155 −16.650 −15.283 1.00 18.17 BBBB ATOM 3977 O VAL B 184 17.931 −16.882 −14.092 1.00 16.37 BBBB ATOM 3978 N ARG B 185 17.244 −16.771 −16.245 1.00 17.91 BBBB ATOM 3979 CA ARG B 185 15.873 −17.216 −16.011 1.00 17.62 BBBB ATOM 3980 CB ARG B 185 14.966 −16.622 −17.092 1.00 17.65 BBBB ATOM 3981 CG ARG B 185 15.036 −15.110 −17.160 1.00 18.62 BBBB ATOM 3982 CD ARG B 185 14.344 −14.624 −18.420 1.00 20.39 BBBB ATOM 3983 NE ARG B 185 14.307 −13.173 −18.516 1.00 19.72 BBBB ATOM 3984 CZ ARG B 185 13.647 −12.520 −19.466 1.00 20.23 BBBB ATOM 3985 NH1 ARG B 185 12.977 −13.197 −20.391 1.00 19.85 BBBB ATOM 3986 NH2 ARG B 185 13.650 −11.197 −19.487 1.00 23.44 BBBB ATOM 3987 C ARG B 185 15.804 −18.740 −16.037 1.00 16.88 BBBB ATOM 3988 O ARG B 185 15.971 −19.367 −17.087 1.00 15.75 BBBB ATOM 3989 N VAL B 186 15.566 −19.326 −14.870 1.00 15.97 BBBB ATOM 3990 CA VAL B 186 15.508 −20.771 −14.741 1.00 16.47 BBBB ATOM 3991 CB VAL B 186 16.259 −21.245 −13.476 1.00 15.51 BBBB ATOM 3992 CG1 VAL B 186 16.316 −22.770 −13.448 1.00 17.66 BBBB ATOM 3993 CG2 VAL B 186 17.652 −20.626 −13.430 1.00 16.97 BBBB ATOM 3994 C VAL B 186 14.076 −21.282 −14.644 1.00 16.41 BBBB ATOM 3995 O VAL B 186 13.343 −20.920 −13.732 1.00 18.33 BBBB ATOM 3996 N LEU B 187 13.695 −22.128 −15.588 1.00 15.92 BBBB ATOM 3997 CA LEU B 187 12.361 −22.710 −15.604 1.00 16.75 BBBB ATOM 3998 CB LEU B 187 11.813 −22.701 −17.035 1.00 16.85 BBBB ATOM 3999 CG LEU B 187 10.445 −23.340 −17.276 1.00 18.63 BBBB ATOM 4000 CD1 LEU B 187 9.368 −22.478 −16.625 1.00 19.42 BBBB ATOM 4001 CD2 LEU B 187 10.198 −23.449 −18.783 1.00 19.11 BBBB ATOM 4002 C LEU B 187 12.450 −24.146 −15.085 1.00 16.85 BBBB ATOM 4003 O LEU B 187 13.115 −24.982 −15.688 1.00 17.18 BBBB ATOM 4004 N VAL B 188 11.788 −24.426 −13.964 1.00 18.20 BBBB ATOM 4005 CA VAL B 188 11.774 −25.775 −13.381 1.00 18.41 BBBB ATOM 4006 CB VAL B 188 11.902 −25.714 −11.842 1.00 18.98 BBBB ATOM 4007 CG1 VAL B 188 12.088 −27.126 −11.270 1.00 18.50 BBBB ATOM 4008 CG2 VAL B 188 13.061 −24.818 −11.449 1.00 18.83 BBBB ATOM 4009 C VAL B 188 10.434 −26.440 −13.739 1.00 19.88 BBBB ATOM 4010 O VAL B 188 9.371 −25.967 −13.336 1.00 20.39 BBBB ATOM 4011 N VAL B 189 10.493 −27.532 −14.496 1.00 21.55 BBBB ATOM 4012 CA VAL B 189 9.298 −28.234 −14.948 1.00 22.11 BBBB ATOM 4013 CB VAL B 189 9.299 −28.342 −16.488 1.00 22.50 BBBB ATOM 4014 CG1 VAL B 189 8.009 −29.013 −16.981 1.00 22.70 BBBB ATOM 4015 CG2 VAL B 189 9.470 −26.943 −17.101 1.00 21.26 BBBB ATOM 4016 C VAL B 189 9.191 −29.639 −14.351 1.00 23.90 BBBB ATOM 4017 O VAL B 189 10.067 −30.478 −14.559 1.00 23.61 BBBB ATOM 4018 N GLY B 190 8.111 −29.887 −13.615 1.00 25.60 BBBB ATOM 4019 CA GLY B 190 7.914 −31.188 −12.994 1.00 27.28 BBBB ATOM 4020 C GLY B 190 6.808 −32.026 −13.604 1.00 29.67 BBBB ATOM 4021 O GLY B 190 6.668 −33.208 −13.283 1.00 29.86 BBBB ATOM 4022 N GLY B 191 6.025 −31.430 −14.497 1.00 30.56 BBBB ATOM 4023 CA GLY B 191 4.935 −32.163 −15.115 1.00 31.94 BBBB ATOM 4024 C GLY B 191 3.676 −32.104 −14.269 1.00 33.11 BBBB ATOM 4025 O GLY B 191 3.691 −31.556 −13.165 1.00 32.41 BBBB ATOM 4026 N SER B 192 2.687 −32.673 −14.779 1.00 34.23 BBBB ATOM 4027 CA SER B 192 1.313 −32.665 −14.064 1.00 35.91 BBBB ATOM 4028 CB SER B 192 0.283 −33.532 −14.801 1.00 36.87 BBBB ATOM 4029 OG SER B 192 0.702 −34.887 −14.877 1.00 39.58 BBBB ATOM 4030 C SER B 192 1.419 −33.128 −12.609 1.00 36.41 BBBB ATOM 4031 O SER B 192 0.862 −32.499 −11.714 1.00 35.78 BBBB ATOM 4032 N GLN B 193 2.134 −34.225 −12.380 1.00 37.60 BBBB ATOM 4033 CA GLN B 193 2.292 −34.763 −11.033 1.00 38.53 BBBB ATOM 4034 CB GLN B 193 2.584 −36.263 −11.096 1.00 41.10 BBBB ATOM 4035 CG GLN B 193 1.501 −37.082 − 11.779 1.00 45.38 BBBB ATOM 4036 CD GLN B 193 0.152 −36.948 − 11.099 1.00 47.81 BBBB ATOM 4037 OE1 GLN B 193 −0.484 −35.892 − 11.149 1.00 49.50 BBBB ATOM 4038 NE2 GLN B 193 −0.290 −38.023 − 10.452 1.00 49.36 BBBB ATOM 4039 C GLN B 193 3.405 −34.072 − 10.260 1.00 37.76 BBBB ATOM 4040 O GLN B 193 3.458 −34.146 −9.030 1.00 37.02 BBBB ATOM 4041 N GLY B 194 4.291 −33.398 − 10.986 1.00 36.47 BBBB ATOM 4042 CA GLY B 194 5.398 −32.711 − 10.350 1.00 35.02 BBBB ATOM 4043 C GLY B 194 6.584 −33.630 − 10.146 1.00 34.51 BBBB ATOM 4044 O GLY B 194 6.442 −34.851 − 10.191 1.00 34.26 BBBB ATOM 4045 N ALA B 195 7.761 −33.045 −9.938 1.00 33.54 BBBB ATOM 4046 CA ALA B 195 8.977 −33.819 −9.709 1.00 33.12 BBBB ATOM 4047 CB ALA B 195 10.073 −33.387 − 10.679 1.00 33.17 BBBB ATOM 4048 C ALA B 195 9.423 −33.590 −8.267 1.00 32.87 BBBB ATOM 4049 O ALA B 195 9.955 −32.533 −7.923 1.00 31.47 BBBB ATOM 4050 N ALA B 196 9.195 −34.592 −7.426 1.00 32.81 BBBB ATOM 4051 CA ARG B 196 9.538 −34.512 −6.010 1.00 32.63 BBBB ATOM 4052 CB ARG B 196 9.373 −35.891 −5.361 1.00 35.51 BBBB ATOM 4053 CG ARG B 196 10.382 −36.954 −5.830 1.00 39.68 BBBB ATOM 4054 CD ARG B 196 10.317 −37.224 −7.329 1.00 41.52 BBBB ATOM 4055 NE ARG B 196 9.007 −37.722 −7.738 1.00 43.02 BBBB ATOM 4056 CZ ARG B 196 8.661 −37.955 −8.997 1.00 42.91 BBBB ATOM 4057 NH1 ARG B 196 9.527 −37.735 −9.975 1.00 44.39 BBBB ATOM 4058 NH2 ARG B 196 7.449 −38.408 −9.279 1.00 45.18 BBBB ATOM 4059 C ARG B 196 10.940 −33.977 −5.729 1.00 30.96 BBBB ATOM 4060 O ARG B 196 11.108 −33.035 −4.957 1.00 29.99 BBBB ATOM 4061 N ILE B 197 11.942 −34.573 −6.367 1.00 29.47 BBBB ATOM 4062 CA ILE B 197 13.329 −34.168 −6.164 1.00 28.10 BBBB ATOM 4063 CB ILE B 197 14.284 −35.109 −6.946 1.00 28.46 BBBB ATOM 4064 CG2 ILE B 197 13.984 −35.041 −8.430 1.00 27.99 BBBB ATOM 4065 CG1 ILE B 197 15.742 −34.749 −6.657 1.00 28.64 BBBB ATOM 4066 CD1 ILE B 197 16.212 −35.158 −5.281 1.00 30.51 BBBB ATOM 4067 C ILE B 197 13.579 −32.703 −6.554 1.00 27.65 BBBB ATOM 4068 O ILE B 197 14.378 −32.013 −5.921 1.00 27.21 BBBB ATOM 4069 N LEU B 198 12.897 −32.223 −7.590 1.00 27.07 BBBB ATOM 4070 CA LEU B 198 13.069 −30.833 −8.003 1.00 26.58 BBBB ATOM 4071 CB LEU B 198 12.504 −30.616 −9.412 1.00 25.88 BBBB ATOM 4072 CG LEU B 198 13.196 −31.408 − 10.524 1.00 25.40 BBBB ATOM 4073 CD1 LEU B 198 12.625 −31.007 − 11.874 1.00 26.54 BBBB ATOM 4074 CD2 LEU B 198 14.692 −31.146 − 10.493 1.00 25.94 BBBB ATOM 4075 C LEU B 198 12.388 −29.893 −7.006 1.00 26.41 BBBB ATOM 4076 O LEU B 198 12.930 −28.835 −6.667 1.00 26.35 BBBB ATOM 4077 N ASN B 199 11.205 −30.274 −6.532 1.00 26.01 BBBB ATOM 4078 CA ASN B 199 10.497 −29.447 −5.563 1.00 27.07 BBBB ATOM 4079 CB ASN B 199 9.123 −30.035 −5.238 1.00 26.63 BBBB ATOM 4080 CG ASN B 199 8.212 −30.050 −6.434 1.00 27.62 BBBB ATOM 4081 OD1 ASN B 199 8.519 −29.434 −7.460 1.00 26.33 BBBB ATOM 4082 ND2 ASN B 199 7.080 −30.749 −6.320 1.00 24.20 BBBB ATOM 4083 C ASN B 199 11.308 −29.319 −4.282 1.00 27.65 BBBB ATOM 4084 O ASN B 199 11.207 −28.321 −3.581 1.00 28.19 BBBB ATOM 4085 N GLN B 200 12.124 −30.328 −3.994 1.00 28.38 BBBB ATOM 4086 CA GLN B 200 12.955 −30.326 −2.794 1.00 30.10 BBBB ATOM 4087 CB GLN B 200 13.158 −31.764 −2.301 1.00 31.91 BBBB ATOM 4088 CG GLN B 200 11.883 −32.453 −1.827 1.00 35.02 BBBB ATOM 4089 CD GLN B 200 12.056 −33.956 −1.632 1.00 37.49 BBBB ATOM 4090 CO1 GLN B 200 11.204 −34.619 −1.032 1.00 38.76 BBBB ATOM 4091 NE2 GLN B 200 13.155 −34.502 −2.151 1.00 37.28 BBBB ATOM 4092 C GLN B 200 14.319 −29.675 −3.011 1.00 30.18 BBBB ATOM 4093 C GLN B 200 14.834 −28.975 −2.135 1.00 31.13 BBBB ATOM 4094 N THR B 201 14.897 −29.884 −4.187 1.00 28.94 BBBB ATOM 4095 CA THR B 201 16.215 −29.345 −4.474 1.00 27.34 BBBB ATOM 4096 CB THR B 201 16.915 −30.181 −5.567 1.00 28.81 BBBB ATOM 4097 OG1 THR B 201 16.988 −31.553 −5.149 1.00 28.92 BBBB ATOM 4098 CG2 THR B 201 18.331 −29.654 −5.817 1.00 28.29 BBBB ATOM 4099 C THR B 201 16.313 −27.871 −4.869 1.00 25.78 BBBB ATOM 4100 O THR B 201 17.137 −27.138 −4.331 1.00 24.91 BBBB ATOM 4101 N MET B 202 15.479 −27.430 −5.800 1.00 24.08 BBBB ATOM 4102 CA MET B 202 15.567 −26.048 −6.268 1.00 23.68 BBBB ATOM 4103 CB MET B 202 14.558 −25.827 −7.397 1.00 22.29 BBBB ATOM 4104 CG MET B 202 14.856 −26.685 −8.633 1.00 22.80 BBBB ATOM 4105 SD MET B 202 16.590 −26.614 −9.190 1.00 25.93 BBBB ATOM 4106 CE MET B 202 16.814 −24.877 −9.345 1.00 22.63 BBBB ATOM 4107 C MET B 202 15.489 −24.926 −5.229 1.00 23.47 BBBB ATOM 4108 O MET B 202 16.189 −23.929 −5.354 1.00 24.40 BBBB ATOM 4109 N PRO B 203 14.636 −25.059 −4.192 1.00 24.12 BBBB ATOM 4110 CD PRO B 203 13.518 −25.991 −3.970 1.00 22.27 BBBB ATOM 4111 CA PRO B 203 14.608 −23.963 −3.220 1.00 23.84 BBBB ATOM 4112 CB PRO B 203 13.553 −24.424 −2.217 1.00 24.46 BBBB ATOM 4113 CG PRO B 203 12.593 −25.178 −3.084 1.00 24.04 BBBB ATOM 4114 C PRO B 203 15.987 −23.731 −2.573 1.00 24.07 BBBB ATOM 4115 O PRO B 203 16.395 −22.593 −2.343 1.00 23.18 BBBB ATOM 4116 N GLN B 204 16.706 −24.814 −2.290 1.00 25.26 BBBB ATOM 4117 CA GLN B 204 18.033 −24.708 −1.684 1.00 26.34 BBBB ATOM 4118 CB GLN B 204 18.474 −26.078 −1.157 1.00 28.67 BBBB ATOM 4119 CG GLN B 204 17.555 −26.626 −0.065 1.00 33.65 BBBB ATOM 4120 CD GLN B 204 17.885 −28.059 0.328 1.00 37.09 BBBB ATOM 4121 OE1 GLN B 204 18.991 −28.354 0.792 1.00 39.30 BBBB ATOM 4122 NE2 GLN B 204 16.924 −28.960 0.140 1.00 38.32 BBBB ATOM 4123 C GLN B 204 19.030 −24.177 −2.717 1.00 25.36 BBBB ATOM 4124 O GLN B 204 19.985 −23.466 −2.385 1.00 24.98 BBBB ATOM 4125 N VAL B 205 18.806 −24.522 −3.978 1.00 24.46 BBBB ATOM 4126 CA VAL B 205 19.672 −24.033 −5.043 1.00 24.44 BBBB ATOM 4127 CB VAL B 205 19.288 −24.634 −6.409 1.00 24.84 BBBB ATOM 4128 CG1 VAL B 205 20.039 −23.906 −7.534 1.00 23.72 BBBB ATOM 4129 CG2 VAL B 205 19.614 −26.110 −6.428 1.00 22.91 BBBB ATOM 4130 C VAL B 205 19.511 −22.515 −5.110 1.00 23.79 BBBB ATOM 4131 O VAL B 205 20.487 −21.789 −5.270 1.00 25.25 BBBB ATOM 4132 N ALA B 206 18.273 −22.044 −4.972 1.00 24.12 BBBB ATOM 4133 CA ALA B 206 17.980 − 20.610 −5.013 1.00 22.84 BBBB ATOM 4134 CB ALA B 206 16.466 − 20.377 −4.908 1.00 21.55 BBBB ATOM 4135 C ALA B 206 18.700 − 19.862 −3.890 1.00 24.09 BBBB ATOM 4136 O ALA B 206 19.174 − 18.740 −4.081 1.00 24.90 BBBB ATOM 4137 N ALA B 207 18.768 − 20.477 −2.713 1.00 25.15 BBBB ATOM 4138 CA ALA B 207 19.442 − 19.857 −1.576 1.00 26.65 BBBB ATOM 4139 CB ALA B 207 19.260 − 20.710 −0.324 1.00 27.83 BBBB ATOM 4140 C ALA B 207 20.924 − 19.686 −1.879 1.00 26.96 BBBB ATOM 4141 O ALA B 207 21.537 − 18.693 −1.493 1.00 27.82 BBBB ATOM 4142 N LYS B 208 21.498 − 20.651 −2.586 1.00 27.19 BBBB ATOM 4143 CA LYS B 208 22.915 − 20.595 −2.919 1.00 28.31 BBBB ATOM 4144 CB LYS B 208 23.432 −21.989 −3.300 1.00 29.85 BBBB ATOM 4145 CG LYS B 208 23.030 −23.088 −2.329 1.00 32.97 BBBB ATOM 4146 CD LYS B 208 23.264 −22.667 −0.886 1.00 35.74 BBBB ATOM 4147 CE LYS B 208 22.689 −23.689 0.084 1.00 37.28 BBBB ATOM 4148 NZ LYS B 208 21.227 −23.899 −0.135 1.00 35.29 BBBB ATOM 4149 C LYS B 208 23.237 − 19.624 −4.050 1.00 27.83 BBBB ATOM 4150 O LYS B 208 24.286 − 18.978 −4.033 1.00 27.46 BBBB ATOM 4151 N LEU B 209 22.341 − 19.517 −5.028 1.00 26.04 BBBB ATOM 4152 CA LEU B 209 22.577 − 18.640 −6.171 1.00 25.68 BBBB ATOM 4153 CB LEU B 209 21.975 − 19.268 −7.435 1.00 25.08 BBBB ATOM 4154 CG LEU B 209 22.534 − 20.638 −7.844 1.00 25.01 BBBB ATOM 4155 CD1 LEU B 209 21.797 −21.151 −9.074 1.00 25.67 BBBB ATOM 4156 CD2 LEU B 209 24.029 − 20.528 −8.119 1.00 25.13 BBBB ATOM 4157 C LEU B 209 22.075 − 17.200 −6.007 1.00 25.59 BBBB ATOM 4158 O LEU B 209 22.496 − 16.313 −6.742 1.00 25.26 BBBB ATOM 4159 N GLY B 210 21.185 − 16.970 −5.045 1.00 26.27 BBBB ATOM 4160 CA GLY B 210 20.675 − 15.628 −4.804 1.00 26.56 BBBB ATOM 4161 C GLY B 210 20.238 − 14.836 −6.030 1.00 27.75 BBBB ATOM 4162 O GLY B 210 19.518 − 15.349 −6.889 1.00 27.68 BBBB ATOM 4163 N ASP B 211 20.696 − 13.585 −6.105 1.00 27.93 BBBB ATOM 4164 CA ASP B 211 20.370 − 12.647 −7.190 1.00 28.28 BBBB ATOM 4165 CB ASP B 211 21.011 − 11.283 −6.906 1.00 29.89 BBBB ATOM 4166 CG ASP B 211 20.351 − 10.545 −5.768 1.00 31.43 BBBB ATOM 4167 OD1 ASP B 211 20.864 −9.469 −5.398 1.00 32.43 BBBB ATOM 4168 OD2 ASP B 211 19.323 − 11.025 −5.249 1.00 33.41 BBBB ATOM 4169 C ASP B 211 20.768 − 13.035 −8.615 1.00 27.77 BBBB ATOM 4170 O ASP B 211 20.320 − 12.397 −9.578 1.00 26.32 BBBB ATOM 4171 N SER B 212 21.616 − 14.048 −8.753 1.00 25.75 BBBB ATOM 4172 CA SER B 212 22.098 − 14.474 − 10.067 1.00 25.73 BBBB ATOM 4173 CB SER B 212 23.331 − 15.376 −9.904 1.00 26.63 BBBB ATOM 4174 OG SER B 212 22.971 − 16.596 −9.282 1.00 26.71 BBBB ATOM 4175 C SER B 212 21.062 − 15.185 − 10.943 1.00 23.61 BBBB ATOM 4176 O SER B 212 21.262 − 15.334 − 12.147 1.00 22.28 BBBB ATOM 4177 N VAL B 213 19.969 − 15.644 − 10.344 1.00 23.16 BBBB ATOM 4178 CA VAL B 213 18.925 − 16.308 − 11.116 1.00 20.76 BBBB ATOM 4179 CB VAL B 213 18.952 − 17.867 − 10.989 1.00 21.69 BBBB ATOM 4180 CG1 VAL B 213 20.318 − 18.423 − 11.375 1.00 19.84 BBBB ATOM 4181 CG2 VAL B 213 18.564 − 18.288 −9.576 1.00 20.36 BBBB ATOM 4182 C VAL B 213 17.535 − 15.871 − 10.677 1.00 21.41 BBBB ATOM 4183 O VAL B 213 17.328 − 15.396 −9.554 1.00 20.58 BBBB ATOM 4184 N THR B 214 16.593 − 16.021 − 11.595 1.00 19.82 BBBB ATOM 4185 CA THR B 214 15.204 − 15.726 − 11.337 1.00 19.60 BBBB ATOM 4186 CB THR B 214 14.718 − 14.478 − 12.126 1.00 21.35 BBBB ATOM 4187 OG1 THR B 214 13.323 − 14.273 − 11.870 1.00 21.93 BBBB ATOM 4188 CG2 THR B 214 14.983 − 14.633 − 13.622 1.00 19.52 BBBB ATOM 4189 C THR B 214 14.543 − 17.021 − 11.791 1.00 20.24 BBBB ATOM 4190 O THR B 214 14.803 − 17.533 − 12.893 1.00 18.70 BBBB ATOM 4191 N ILE B 215 13.706 − 17.569 − 10.921 1.00 19.21 BBBB ATOM 4192 CA ILE B 215 13.076 − 18.850 − 11.169 1.00 18.75 BBBB ATOM 4193 CB ILE B 215 13.417 − 19.828 − 10.008 1.00 18.82 BBBB ATOM 4194 CG2 ILE B 215 12.690 −21.157 − 10.194 1.00 19.53 BBBB ATOM 4195 CG1 ILE B 215 14.934 − 20.030 −9.931 1.00 19.76 BBBB ATOM 4196 CD1 ILE B 215 15.421 − 20.656 −8.600 1.00 19.40 BBBB ATOM 4197 C ILE B 215 11.568 − 18.837 − 11.315 1.00 19.26 BBBB ATOM 4198 O ILE B 215 10.874 − 18.025 − 10.699 1.00 18.28 BBHB ATOM 4199 N TRP B 216 11.089 − 19.737 − 12.167 1.00 18.93 BBBB ATOM 4200 CA TRP B 216 9.661 − 19.973 − 12.378 1.00 19.34 BBBB ATOM 4201 CB TRP B 216 9.222 − 19.631 − 13.797 1.00 18.97 BBBB ATOM 4202 CG TRP B 216 7.757 − 19.897 − 14.065 1.00 20.09 BBBB ATOM 4203 CD2 TRP B 216 7.015 − 19.467 − 15.211 1.00 19.61 BBBB ATOM 4204 CE2 TRP B 216 5.705 − 19.988 − 15.085 1.00 19.98 BBBB ATOM 4205 CE3 TRP B 216 7.329 − 18.690 − 16.333 1.00 19.39 BBBB ATOM 4206 CD1 TRP B 216 6.888 − 20.639 − 13.303 1.00 19.30 BBBB ATOM 4207 NE1 TRP B 216 5.653 − 20.700 − 13.914 1.00 20.95 BBBB ATOM 4208 CZ2 TRP B 216 4.713 − 19.759 − 16.043 1.00 22.06 BBBB ATOM 4209 CZ3 TRP B 216 6.336 − 18.459 − 17.288 1.00 20.42 BBBB ATOM 4210 CH2 TRP B 216 5.047 − 18.993 − 17.134 1.00 21.16 BBBB ATOM 4211 C TRP B 216 9.629 −21.479 − 12.176 1.00 19.95 BBBB ATOM 4212 O TRP B 216 10.114 −22.241 − 13.010 1.00 19.91 BBBB ATOM 4213 N HIS B 217 9.067 −21.897 − 11.050 1.00 21.62 BBBB ATOM 4214 CA HIS B 217 9.015 −23.303 − 10.680 1.00 21.06 BBBB ATOM 4215 CB HIS B 217 9.553 −23.419 −9.242 1.00 20.56 BBBB ATOM 4216 CG HIS B 217 9.717 −24.824 −8.747 1.00 21.95 BBBB ATOM 4217 CD2 HIS B 217 8.915 −25.910 −8.846 1.00 22.12 BBBB ATOM 4218 ND1 HIS B 217 10.807 −25.219 −8.002 1.00 23.39 BBBB ATOM 4219 CE1 HIS B 217 10.670 −26.490 −7.663 1.00 21.82 BBBB ATOM 4220 NE2 HIS B 217 9.530 −26.933 −8.162 1.00 22.14 BHBB ATOM 4221 C HIS B 217 7.596 −23.870 − 10.795 1.00 21.27 BBBB ATOM 4222 O HIS B 217 6.655 −23.334 − 10.214 1.00 21.69 BBBB ATOM 4223 N GLN B 218 7.448 −24.940 − 11.567 1.00 20.83 BBBB ATOM 4224 CA GLN B 218 6.149 −25.594 − 11.735 1.00 24.30 BBHB ATOM 4225 CB GLN B 218 5.915 −25.935 − 13.206 1.00 23.84 BBBB ATOM 4226 CG GLN B 218 4.561 −26.558 − 13.495 1.00 25.91 BBBB ATOM 4227 CD GLN B 218 4.637 −28.060 − 13.673 1.00 26.52 BBBB ATOM 4228 OE1 GLN B 218 3.757 −28.793 − 13.214 1.00 28.05 BBBB ATOM 4229 NE2 GLN B 218 5.680 −28.529 − 14.360 1.00 25.20 BBBB ATOM 4230 C GLN B 218 6.173 −26.854 − 10.854 1.00 24.64 BBBB ATOM 4231 O GLN B 218 6.780 −27.866 − 11.199 1.00 25.73 BBBB ATOM 4232 N SER B 219 5.502 −26.756 −9.709 1.00 26.38 BBBB ATOM 4233 CA SER B 219 5.463 −27.800 −8.684 1.00 26.73 BBBB ATOM 4234 CB SER B 219 4.947 −27.188 −7.380 1.00 28.26 BBBB ATOM 4235 OG SER B 219 3.563 −26.881 −7.488 1.00 26.22 BBBB ATOM 4236 C SER B 219 4.689 −29.096 −8.914 1.00 27.58 BBBB ATOM 4237 O SER B 219 5.014 −30.122 −8.320 1.00 26.39 BBBB ATOM 4238 N GLY B 220 3.662 −29.054 −9.750 1.00 28.58 BBBB ATOM 4239 CA GLY B 220 2.855 −30.242 −9.961 1.00 30.53 BBBB ATOM 4240 C GLY B 220 1.596 −30.110 −9.111 1.00 31.96 BBBB ATOM 4241 O GLY B 220 1.523 −29.248 −8.233 1.00 30.92 BBBB ATOM 4242 N LYS B 221 0.608 −30.965 −9.358 1.00 33.93 BBBB ATOM 4243 CA LYS B 221 −0.657 −30.914 −8.628 1.00 35.12 BBBB ATOM 4244 CB LYS B 221 −1.573 −32.049 −9.094 1.00 37.88 BBBB ATOM 4245 CG LYS B 221 −2.942 −32.055 −8.427 1.00 40.51 BBBB ATOM 4246 CD LYS B 221 −3.792 −33.215 −8.934 1.00 42.62 BBBB ATOM 4247 CE LYS B 221 −5.162 −33.249 −8.260 1.00 43.67 BBBB ATOM 4248 NZ LYS B 221 −6.002 −34.383 −8.763 1.00 45.38 BBBB ATOM 4249 C LYS B 221 −0.545 −30.950 −7.103 1.00 35.13 BBBB ATOM 4250 O LYS B 221 0.110 −31.823 −6.531 1.00 34.60 BBBB ATOM 4251 N GLY B 222 −1.187 −29.979 −6.461 1.00 34.79 BBBB ATOM 4252 CA GLY B 222 −1.195 −29.899 −5.011 1.00 35.34 BBBB ATOM 4253 C GLY B 222 0.111 −29.594 −4.299 1.00 35.61 BBBB ATOM 4254 O GLY B 222 0.163 −29.678 −3.071 1.00 35.51 BBBB ATOM 4255 N SER B 223 1.158 −29.234 −5.038 1.00 34.65 BBBB ATOM 4256 CA SER B 223 2.451 −28.934 −4.418 1.00 33.98 BBBB ATOM 4257 CB SER B 223 3.552 −29.781 −5.062 1.00 35.02 BBBB ATOM 4258 OG SER B 223 3.303 −31.168 −4.897 1.00 36.07 BBBB ATOM 4259 C SER B 223 2.839 −27.454 −4.504 1.00 33.55 BBBB ATOM 4260 O SER B 223 3.930 −27.063 −4.086 1.00 31.72 BBBB ATOM 4261 N GLN B 224 1.941 −26.639 −5.044 1.00 33.22 BBBB ATOM 4262 CA GLN B 224 2.187 −25.208 −5.186 1.00 33.71 BBBB ATOM 4263 CB GLN B 224 0.954 −24.539 −5.799 1.00 35.45 BBBB ATOM 4264 CG GLN B 224 1.160 −23.120 −6.337 1.00 37.82 BBBB ATOM 4265 CD GLN B 224 1.344 −22.076 −5.249 1.00 40.08 BBBB ATOM 4266 CE1 GLN B 224 0.669 −22.111 −4.217 1.00 40.97 BBBB ATOM 4267 NE2 GLN B 224 2.244 −21.124 −5.486 1.00 40.08 BBBB ATOM 4268 C GLN B 224 2.510 −24.560 −3.840 1.00 33.86 BBBB ATOM 4269 O GLN B 224 3.512 −23.856 −3.697 1.00 33.38 BBBB ATOM 4270 N GLN B 225 1.659 −24.814 −2.850 1.00 33.06 BBBB ATOM 4271 CA GLN B 225 1.823 −24.239 −1.519 1.00 32.32 BBBB ATOM 4272 CB GLN B 225 0.624 −24.619 −0.640 1.00 35.12 BBBB ATOM 4273 CG GLN B 225 −0.743 −24.143 −1.151 1.00 36.85 BBBB ATOM 4274 CD GLN B 225 −1.144 −24.751 −2.495 1.00 39.09 BBBB ATOM 4275 CE1 GLN B 225 −0.914 −25.937 −2.759 1.00 39.42 BBBB ATOM 4276 NE2 GLN B 225 −1.768 −23.937 −3.345 1.00 40.13 BBBB ATOM 4277 C GLN B 225 3.117 −24.606 −0.788 1.00 30.73 BBBB ATOM 4278 O GLN B 225 3.766 −23.742 −0.202 1.00 30.36 BBBB ATOM 4279 N SER B 226 3.494 −25.878 −0.817 1.00 29.26 BBBB ATOM 4280 CA SER B 226 4.701 −26.309 −0.122 1.00 28.30 BBBB ATOM 4281 CB SER B 226 4.727 −27.834 −0.003 1.00 29.10 BBBB ATOM 4282 OG SER B 226 4.563 −28.461 −1.254 1.00 32.61 BBBB ATOM 4283 C SER B 226 5.991 −25.809 −0.771 1.00 26.41 BBBB ATOM 4284 O SER B 226 6.950 −25.486 −0.073 1.00 25.24 BBBB ATOM 4285 N VAL B 227 6.019 −25.738 −2.099 1.00 25.21 BBBB ATOM 4286 CA VAL B 227 7.214 −25.247 −2.791 1.00 24.28 BBBB ATOM 4287 CB VAL B 227 7.150 −25.527 −4.317 1.00 23.32 BBBB ATOM 4288 CG1 VAL B 227 8.368 −24.914 −5.028 1.00 20.67 BBBB ATOM 4289 CG2 VAL B 227 7.117 −27.024 −4.563 1.00 22.45 BBBB ATOM 4290 C VAL B 227 7.335 −23.743 −2.545 1.00 24.34 BBBB ATOM 4291 O VAL B 227 8.421 −23.240 −2.281 1.00 25.50 BBBB ATOM 4292 N GLU B 228 6.209 −23.035 −2.623 1.00 26.12 BBBB ATOM 4293 CA GLU B 228 6.178 −21.592 −2.387 1.00 27.23 BBBB ATOM 4294 CB GLU B 228 4.735 −21.075 −2.476 1.00 28.60 BBBB ATOM 4295 CG GLU B 228 4.558 − 19.586 −2.184 1.00 30.24 BBBB ATOM 4296 CD GLU B 228 4.938 − 18.688 −3.356 1.00 31.99 BBBB ATOM 4297 OE1 GLU B 228 5.012 − 17.452 −3.159 1.00 31.68 BBBB ATOM 4298 OE2 GLU B 228 5.154 − 19.212 −4.471 1.00 32.04 BBBB ATOM 4299 C GLU B 228 6.746 −21.327 −0.994 1.00 27.95 BBBB ATOM 4300 O GLU B 228 7.511 − 20.383 −0.787 1.00 27.32 BBBB ATOM 4301 N GLN B 229 6.374 −22.178 −0.041 1.00 28.66 BBBB ATOM 4302 CA GLN B 229 6.853 −22.046 1.329 1.00 28.38 BBBB ATOM 4303 CB GLN B 229 6.082 −22.990 2.261 1.00 31.03 BBBB ATOM 4304 CG GLN B 229 6.570 −22.946 3.700 1.00 35.48 BBBB ATOM 4305 CD GLN B 229 5.780 −23.860 4.615 1.00 38.01 BBBB ATOM 4306 OE1 GLN B 229 4.548 −23.810 4.645 1.00 39.26 BBBB ATOM 4307 NE2 GLN B 229 6.484 −24.697 5.370 1.00 38.61 BBBB ATOM 4308 C GLN B 229 8.338 −22.362 1.407 1.00 27.09 BBBB ATOM 4309 O GLN B 229 9.084 −21.697 2.124 1.00 28.29 BBBB ATOM 4310 N ALA B 230 8.771 −23.385 0.677 1.00 26.97 BBBB ATOM 4311 CA ALA B 230 10.185 −23.754 0.682 1.00 26.18 BBBB ATOM 4312 CB ALA B 230 10.412 −24.984 −0.184 1.00 25.07 BBBB ATOM 4313 C ALA B 230 11.054 −22.588 0.192 1.00 26.36 BBBB ATOM 4314 O ALA B 230 12.119 −22.317 0.755 1.00 25.04 BBBB ATOM 4315 N TYR B 231 10.605 −21.895 −0.854 1.00 25.85 BBBB ATOM 4316 CA TYR B 231 11.371 − 20.766 −1.366 1.00 25.47 BBBB ATOM 4317 CB TYR B 231 10.762 − 20.248 −2.678 1.00 24.72 BBBB ATOM 4318 CG TYR B 231 11.236 −21.014 −3.905 1.00 23.66 BBBB ATOM 4319 CD1 TYR B 231 12.546 − 20.869 −4.381 1.00 23.97 BBBB ATOM 4320 CE1 TYR B 231 13.006 −21.599 −5.488 1.00 21.40 BBBB ATOM 4321 CD2 TYR B 231 10.393 −21.905 −4.567 1.00 22.63 BBBB ATOM 4322 CE2 TYR B 231 10.841 −22.641 −5.681 1.00 22.71 BBBB ATOM 4323 CZ TYR B 231 12.151 −22.480 −6.128 1.00 21.91 BBBB ATOM 4324 OH TYR B 231 12.600 −23.214 −7.199 1.00 21.69 BBBB ATOM 4325 C TYR B 231 11.450 − 19.639 −0.336 1.00 26.53 BBBB ATOM 4326 O TYR B 231 12.498 − 19.011 −0.175 1.00 26.32 BBBB ATOM 4327 N ALA B 232 10.345 − 19.380 0.361 1.00 26.28 BBBB ATOM 4328 CA ALA B 232 10.342 − 18.322 1.368 1.00 27.51 BBBB ATOM 4329 CB ALA B 232 8.930 − 18.109 1.910 1.00 28.09 BBBB ATOM 4330 C ALA B 232 11.303 − 18.695 2.499 1.00 28.03 BBBB ATOM 4331 O ALA B 232 12.069 − 17.858 2.983 1.00 27.93 BBBB ATOM 4332 N GLU B 233 11.263 − 19.958 2.911 1.00 29.43 BBBB ATOM 4333 CA GLU B 233 12.145 − 20.441 3.966 1.00 30.87 BBBB ATOM 4334 CB GLU B 233 11.772 −21.877 4.344 1.00 33.60 BBBB ATOM 4335 CG GLU B 233 10.491 −21.973 5.170 1.00 37.67 BBBB ATOM 4336 CD GLU B 233 10.077 −23.404 5.461 1.00 40.35 BBBB ATOM 4337 OE1 GLU B 233 10.964 −24.283 5.525 1.00 42.97 BBBB ATOM 4338 OE2 GLU B 233 8.864 −23.649 5.641 1.00 41.95 BBBB ATOM 4339 C GLU B 233 13.606 − 20.369 3.530 1.00 30.58 BBBB ATOM 4340 O GLU B 233 14.499 − 20.202 4.359 1.00 30.82 BBBB ATOM 4341 N ALA B 234 13.850 − 20.485 2.227 1.00 29.17 BBBB ATOM 4342 CA ALA B 234 15.215 − 20.417 1.714 1.00 28.48 BBBB ATOM 4343 CB ALA B 234 15.310 −21.110 0.354 1.00 27.71 BBBB ATOM 4344 C ALA B 234 15.649 − 18.961 1.588 1.00 27.73 BBBB ATOM 4345 O ALA B 234 16.787 − 18.677 1.213 1.00 27.34 BBBB ATOM 4346 N GLY B 235 14.731 − 18.045 1.890 1.00 26.74 BBBB ATOM 4347 CA GLY B 235 15.033 − 16.627 1.815 1.00 26.23 BBBB ATOM 4348 C GLY B 235 14.946 − 16.009 0.426 1.00 26.13 BBBB ATOM 4349 O GLY B 235 15.483 − 14.924 0.198 1.00 25.67 BBBB ATOM 4350 N GLN B 236 14.284 − 16.696 −0.502 1.00 25.36 BBBB ATOM 4351 CA GLN B 236 14.121 − 16.198 −1.870 1.00 25.53 BBBB ATOM 4352 CB GLN B 236 14.940 − 17.043 −2.852 1.00 25.84 BBBB ATOM 4353 CG GLN B 236 16.436 − 17.074 −2.603 1.00 27.18 BBBB ATOM 4354 CD GLN B 236 17.080 − 15.705 −2.661 1.00 28.96 BBBB ATOM 4355 OE1 GLN B 236 16.686 − 14.850 −3.456 1.00 30.03 BBBB ATOM 4356 NE2 GLN B 236 18.092 − 15.495 −1.829 1.00 29.39 BBBB ATOM 4357 C GLN B 236 12.641 − 16.298 −2.232 1.00 24.12 BBBB ATOM 4358 O GLN B 236 12.262 − 17.002 −3.167 1.00 23.31 BBBB ATOM 4359 N PRO B 237 11.783 − 15.578 −1.497 1.00 24.40 BBBB ATOM 4360 CD PRO B 237 12.143 − 14.580 −0.473 1.00 24.52 BBBB ATOM 4361 CA PRO B 237 10.336 − 15.587 −1.720 1.00 24.65 BBBB ATOM 4362 CB PRO B 237 9.808 − 14.798 −0.527 1.00 25.37 BBBB ATOM 4363 CG PRO B 237 10.862 − 13.773 −0.340 1.00 25.24 BBBB ATOM 4364 C PRO B 237 9.837 − 15.012 −3.043 1.00 25.33 BBBB ATOM 4365 O PRO B 237 8.720 − 15.313 −3.465 1.00 24.93 BBBB ATOM 4366 N GLN B 238 10.663 − 14.197 −3.690 1.00 24.47 BBBB ATOM 4367 CA GLN B 238 10.277 − 13.558 −4.945 1.00 24.29 BBBB ATOM 4368 CB GLN B 238 11.281 − 12.455 −5.306 1.00 23.76 BBBB ATOM 4369 CG GLN B 238 12.622 − 12.945 −5.852 1.00 25.22 BBBB ATOM 4370 CD GLN B 238 13.535 − 13.523 −4.783 1.00 26.90 BBBB ATOM 4371 OE1 GLN B 238 13.188 − 13.550 −3.600 1.00 28.05 BBBB ATOM 4372 NE2 GLN B 238 14.712 − 13.983 −5.195 1.00 25.61 BBBB ATOM 4373 C GLN B 238 10.108 − 14.489 −6.143 1.00 23.41 BBBB ATOM 4374 O GLN B 238 9.485 − 14.112 −7.139 1.00 20.49 BBBB ATOM 4375 N HIS B 239 10.655 − 15.700 −6.069 1.00 22.66 BBBB ATOM 4376 CA HIS B 239 10.526 − 16.608 −7.201 1.00 22.08 BBBB ATOM 4377 CB HIS B 239 11.432 − 17.829 −7.008 1.00 22.41 BBBB ATOM 4378 CG HIS B 239 12.891 − 17.488 −6.998 1.00 20.93 BBBB ATOM 4379 CD2 HIS B 239 13.869 − 17.774 −6.104 1.00 20.09 BBBB ATOM 4380 ND1 HIS B 239 13.488 − 16.743 −7.992 1.00 20.30 BBBB ATOM 4381 CE1 HIS B 239 14.769 − 16.582 −7.711 1.00 22.38 BBBB ATOM 4382 NE2 HIS B 239 15.025 −17.197 −6.569 1.00 19.62 BBBB ATOM 4383 C HIS B 239 9.076 − 17.024 −7.433 1.00 22.98 BBBB ATOM 4384 O HIS B 239 8.293 − 17.161 −6.490 1.00 21.86 BBBB ATOM 4385 N LYS B 240 8.727 − 17.209 −8.703 1.00 21.76 BBBB ATOM 4386 CA LYS B 240 7.375 − 17.589 −9.105 1.00 23.26 BBBB ATOM 4387 CB LYS B 240 7.112 − 17.102 − 10.534 1.00 23.38 BBBB ATOM 4388 CG LYS B 240 5.718 − 17.385 − 11.079 1.00 24.06 BBBB ATOM 4389 CD LYS B 240 5.701 − 17.155 − 12.585 1.00 23.93 BBBB ATOM 4390 CE LYS B 240 4.315 − 17.309 − 13.193 1.00 23.72 BBBB ATOM 4391 NZ LYS B 240 3.478 − 16.129 − 12.884 1.00 21.82 BBBB ATOM 4392 C LYS B 240 7.149 − 19.091 −9.046 1.00 23.38 BBBB ATOM 4393 O LYS B 240 7.922 − 19.871 −9.607 1.00 23.06 BBBB ATOM 4394 N VAL B 241 6.075 − 19.497 −8.378 1.00 23.98 BBBB ATOM 4395 CA VAL B 241 5.740 − 20.911 −8.277 1.00 23.78 BBBB ATOM 4396 CB VAL B 241 5.858 −21.428 −6.833 1.00 24.03 BBBB ATOM 4397 CG1 VAL B 241 5.548 −22.923 −6.803 1.00 24.14 BBBB ATOM 4398 CG2 VAL B 241 7.242 −21.144 −6.281 1.00 23.49 BBBB ATOM 4399 C VAL B 241 4.299 −21.136 −8.723 1.00 24.15 BBBB ATOM 4400 O VAL B 241 3.380 − 20.528 −8.184 1.00 24.63 BBBB ATOM 4401 N THR B 242 4.103 −22.000 −9.710 1.00 24.22 BBBB ATOM 4402 CA THR B 242 2.758 −22.301 − 10.177 1.00 25.93 BBBB ATOM 4403 CB THR B 242 2.513 −21.812 − 11.615 1.00 25.89 BBBB ATOM 4404 OG1 THR B 242 3.466 −22.419 12.492 1.00 27.48 BBBB ATOM 4405 CG2 THR B 242 2.639 − 20.299 − 11.697 1.00 26.82 BBBB ATOM 4406 C THR B 242 2.555 −23.809 − 10.135 1.00 26.29 BBBB ATOM 4407 O THR B 242 3.503 −24.577 − 10.303 1.00 26.75 BBBB ATOM 4408 N GLU B 243 1.319 −24.228 −9.898 1.00 26.70 BBBB ATOM 4409 CA GLU B 243 0.999 −25.651 −9.837 1.00 27.03 BBBB ATOM 4410 CB GLU B 243 −0.473 −25.828 −9.445 1.00 29.00 BBBB ATOM 4411 CG GLU B 243 −0.831 −27.218 −8.962 1.00 30.88 BBBB ATOM 4412 CD GLU B 243 −2.297 −27.341 −8.583 1.00 33.00 BBBB ATOM 4413 OE1 GLU B 243 −2.682 −28.402 −8.048 1.00 33.66 BBBB ATOM 4414 OE2 GLU B 243 −3.063 −26.383 −8.827 1.00 32.17 BBBB ATOM 4415 C GLU B 243 1.256 −26.289 − 11.202 1.00 26.61 BBBB ATOM 4416 O GLU B 243 1.841 −27.370 − 11.304 1.00 26.48 BBBB ATOM 4417 N PHE B 244 0.807 −25.602 − 12.248 1.00 26.54 BBBB ATOM 4418 CA PHE B 244 0.964 −26.068 − 13.620 1.00 26.54 BBBB ATOM 4419 CB PHE B 244 −0.376 −26.553 − 14.186 1.00 29.14 BBBB ATOM 4420 CG PHE B 244 −1.110 −27.531 − 13.307 1.00 30.15 BBBB ATOM 4421 CD1 PHE B 244 −0.622 −28.817 − 13.107 1.00 32.26 BBBB ATOM 4422 CD2 PHE B 244 −2.318 −27.172 − 12.716 1.00 31.10 BBBB ATOM 4423 CE1 PHE B 244 −1.335 −29.744 − 12.328 1.00 33.63 BBBB ATOM 4424 CE2 PHE B 244 −3.040 −28.083 − 11.938 1.00 32.04 BBBB ATOM 4425 CZ PHE B 244 −2.549 −29.371 − 11.744 1.00 32.59 BBBB ATOM 4426 C PHE B 244 1.420 −24.915 − 14.507 1.00 25.60 BBBB ATOM 4427 O PHE B 244 1.604 −23.794 − 14.053 1.00 24.93 BBBB ATOM 4428 N ILE B 245 1.591 −25.223 − 15.786 1.00 27.02 BBBB ATOM 4429 CA ILE B 245 1.932 −24.242 − 16.802 1.00 28.48 BBBB ATOM 4430 CB ILE B 245 3.441 −24.226 − 17.159 1.00 28.41 BBBB ATOM 4431 CG2 ILE B 245 3.676 −23.348 − 18.399 1.00 27.05 BBBB ATOM 4432 CG1 ILE B 245 4.245 −23.663 − 15.983 1.00 27.10 BBBB ATOM 4433 CD1 ILE B 245 5.734 −23.543 − 16.256 1.00 27.28 BBBB ATOM 4434 C ILE B 245 1.127 −24.721 − 18.000 1.00 30.75 BBBB ATOM 4435 O ILE B 245 1.428 −25.753 − 18.595 1.00 31.41 BBBB ATOM 4436 N ASP B 246 0.071 −23.997 − 18.331 1.00 33.46 BBBB ATOM 4437 CA ASP B 246 −0.754 −24.396 − 19.457 1.00 36.00 BBBB ATOM 4438 CB ASP B 246 −2.143 −23.754 − 19.342 1.00 39.42 BBBB ATOM 4439 CG ASP B 246 −2.083 −22.246 − 19.141 1.00 42.83 BBBB ATOM 4440 OD1 ASP B 246 −1.447 −21.795 − 18.162 1.00 44.54 BBBB ATOM 4441 OD2 ASP B 246 −2.678 −21.511 − 19.962 1.00 45.41 BBBB ATOM 4442 C ASP B 246 −0.088 −24.020 − 20.780 1.00 35.70 BBBB ATOM 4443 O ASP B 246 −0.155 −24.768 −21.758 1.00 38.58 BBBB ATOM 4444 N ASP B 247 0.582 −22.876 − 20.794 1.00 33.18 BBBB ATOM 4445 CA ASP B 247 1.245 −22.392 −21.999 1.00 30.74 BBBB ATOM 4446 CB ASP B 247 0.936 − 20.904 −22.182 1.00 29.62 BBBB ATOM 4447 CG ASP B 247 1.344 − 20.380 −23.548 1.00 30.15 BBBB ATOM 4448 OE1 ASP B 247 2.161 −21.036 −24.225 1.00 27.57 BBBB ATOM 4449 OD2 ASP B 247 0.854 − 19.296 −23.935 1.00 29.19 BBBB ATOM 4450 C ASP B 247 2.754 −22.607 −21.892 1.00 28.87 BBBB ATOM 4451 O ASP B 247 3.494 −21.695 −21.525 1.00 27.28 BBBB ATOM 4452 N MET B 248 3.204 −23.818 −22.205 1.00 27.72 BBBB ATOM 4453 CA MET B 248 4.625 −24.136 −22.138 1.00 28.41 BBBB ATOM 4454 CB MET B 248 4.856 −25.623 −22.405 1.00 29.48 BBBB ATOM 4455 CG MET B 248 4.952 −26.469 −21.150 1.00 34.21 BBBB ATOM 4456 SD MET B 248 6.277 −25.936 − 20.049 1.00 38.21 BBBB ATOM 4457 CE MET B 248 5.611 −26.499 − 18.479 1.00 37.90 BBBB ATOM 4458 C MET B 248 5.429 −23.313 −23.132 1.00 27.22 BBBB ATOM 4459 O MET B 248 6.578 −22.965 −22.873 1.00 27.06 BBBB ATOM 4460 N ALA B 249 4.827 −23.009 −24.279 1.00 26.23 BBBB ATOM 4461 CA ALA B 249 5.512 −22.216 −25.290 1.00 24.67 BBBB ATOM 4462 CB ALA B 249 4.625 −22.069 −26.537 1.00 25.39 BBBB ATOM 4463 C ALA B 249 5.870 − 20.843 −24.721 1.00 24.03 BBBB ATOM 4464 O ALA B 249 6.971 − 20.338 −24.932 1.00 23.78 BBBB ATOM 4465 N ALA B 250 4.942 − 20.241 −23.983 1.00 23.39 BBBB ATOM 4466 CA ALA B 250 5.188 − 18.933 −23.390 1.00 21.78 BBBB ATOM 4467 CB ALA B 250 3.898 − 18.376 −22.797 1.00 23.21 BBBB ATOM 4468 C ALA B 250 6.277 − 19.011 −22.313 1.00 21.84 BBBB ATOM 4469 O ALA B 250 7.091 − 18.092 −22.176 1.00 20.78 BBBB ATOM 4470 N ALA B 251 6.291 − 20.099 −21.548 1.00 20.34 BBBB ATOM 4471 CA ALA B 251 7.301 − 20.259 − 20.501 1.00 20.85 BBBB ATOM 4472 CB ALA B 251 6.920 −21.405 − 19.568 1.00 19.79 BBBB ATOM 4473 C ALA B 251 8.685 − 20.512 −21.123 1.00 20.95 BBBB ATOM 4474 O ALA B 251 9.689 − 19.980 − 20.648 1.00 21.14 BBBB ATOM 4475 N TYR B 252 8.723 −21.314 −22.184 1.00 21.27 BBBB ATOM 4476 CA TYR B 252 9.972 −21.616 −22.886 1.00 22.78 BBBB ATOM 4477 CB TYR B 252 9.726 −22.661 −23.980 1.00 21.62 BBBB ATOM 4478 CG TYR B 252 9.662 −24.100 −23.505 1.00 23.34 BBBB ATOM 4479 CD1 TYR B 252 9.003 −25.065 −24.261 1.00 22.88 BBBB ATOM 4480 CE1 TYR B 252 8.961 −26.392 −23.861 1.00 24.81 BBBB ATOM 4481 CD2 TYR B 252 10.288 −24.505 −22.319 1.00 22.30 BBBB ATOM 4482 CE2 TYR B 252 10.253 −25.838 −21.912 1.00 23.56 BBBB ATOM 4483 CZ TYR B 252 9.590 −26.772 −22.687 1.00 24.26 BBBB ATOM 4484 OH TYR B 252 9.554 −28.088 −22.305 1.00 25.57 BBBB ATOM 4485 C TYR B 252 10.566 − 20.354 −23.516 1.00 23.57 BBBB ATOM 4486 O TYR B 252 11.784 − 20.180 −23.550 1.00 23.91 BBBB ATOM 4487 N ALA B 253 9.699 − 19.473 −24.007 1.00 23.22 BBBB ATOM 4488 CA ALA B 253 10.131 − 18.224 −24.636 1.00 23.54 BBBB ATOM 4489 CB ALA B 253 8.931 − 17.512 −25.275 1.00 24.59 BBBB ATOM 4490 C ALA B 253 10.783 − 17.305 −23.617 1.00 23.30 BBBB ATOM 4491 O ALA B 253 11.699 − 16.546 −23.945 1.00 23.04 BBBB ATOM 4492 N TRP B 254 10.299 − 17.369 −22.379 1.00 20.49 BBBB ATOM 4493 CA TRP B 254 10.829 − 16.534 −21.303 1.00 19.76 BBBB ATOM 4494 CB TRP B 254 9.808 − 16.467 − 20.151 1.00 19.57 BBBB ATOM 4495 CG TRP B 254 10.381 − 15.981 − 18.841 1.00 19.57 BBBB ATOM 4496 CD2 TRP B 254 10.870 − 16.796 − 17.762 1.00 19.25 BBBB ATOM 4497 CE2 TRP B 254 11.369 − 15.922 − 16.771 1.00 18.94 BBBB ATOM 4498 CE3 TRP B 254 10.939 − 18.178 − 17.543 1.00 19.18 BBBB ATOM 4499 CD1 TRP B 254 10.591 − 14.691 − 18.470 1.00 19.03 BBBB ATOM 4500 NE1 TRP B 254 11.185 − 14.643 − 17.226 1.00 20.30 BBBB ATOM 4501 CZ2 TRP B 254 11.931 − 16.382 − 15.572 1.00 20.01 BBBB ATOM 4502 CZ3 TRP B 254 11.504 − 18.642 − 16.346 1.00 20.05 BBBB ATOM 4503 CH2 TRP B 254 11.991 − 17.743 − 15.380 1.00 18.31 BBBB ATOM 4504 C TRP B 254 12.156 − 17.059 − 20.755 1.00 19.33 BBBB ATOM 4505 O TRP B 254 13.084 − 16.293 − 20.496 1.00 19.25 BBBB ATOM 4506 N ALA B 255 12.234 − 18.373 − 20.597 1.00 18.90 BBBB ATOM 4507 CA ALA B 255 13.399 − 19.025 − 20.003 1.00 19.51 BBBB ATOM 4508 CB ALA B 255 13.082 − 20.507 − 19.788 1.00 18.83 BBBB ATOM 4509 C ALA B 255 14.737 − 18.901 − 20.713 1.00 18.88 BBBB ATOM 4510 O ALA B 255 14.803 − 18.688 −21.918 1.00 19.40 BBBB ATOM 4511 N ASP B 256 15.803 − 19.036 − 19.927 1.00 19.01 BBBB ATOM 4512 CA ASP B 256 17.176 − 19.026 − 20.434 1.00 17.58 BBBB ATOM 4513 CB ASP B 256 18.078 − 18.185 − 19.534 1.00 18.47 BBBB ATOM 4514 CG ASP B 256 17.954 − 16.699 − 19.795 1.00 18.05 BBBB ATOM 4515 OD1 ASP B 256 17.845 − 15.944 − 18.806 1.00 16.89 BBBB ATOM 4516 OD2 ASP B 256 17.983 − 16.287 − 20.982 1.00 19.53 BBBB ATOM 4517 C ASP B 256 17.657 − 20.481 − 20.379 1.00 18.01 BBBB ATOM 4518 O ASP B 256 18.459 − 20.929 −21.198 1.00 16.11 BBBB ATOM 4519 N VAL B 257 17.147 −21.216 − 19.396 1.00 17.49 BBBB ATOM 4520 CA VAL B 257 17.535 −22.603 − 19.194 1.00 18.53 BBBB ATOM 4521 CB VAL B 257 18.831 −22.681 − 18.332 1.00 17.72 BBBB ATOM 4522 CG1 VAL B 257 18.586 −22.069 − 16.966 1.00 19.19 BBBB ATOM 4523 CG2 VAL B 257 19.286 −24.129 − 18.200 1.00 20.40 BBBB ATOM 4524 C VAL B 257 16.400 −23.363 − 18.501 1.00 18.31 BBBB ATOM 4525 O VAL B 257 15.659 −22.795 − 17.703 1.00 19.74 BBBB ATOM 4526 N VAL B 258 16.263 −24.643 − 18.818 1.00 18.74 BBBB ATOM 4527 CA VAL B 258 15.208 −25.456 − 18.234 1.00 19.32 BBBB ATOM 4528 CB VAL B 258 14.328 −26.100 − 19.337 1.00 19.89 BBBB ATOM 4529 CG1 VAL B 258 13.101 −26.754 − 18.714 1.00 19.81 BBBB ATOM 4530 CG2 VAL B 258 13.907 −25.041 − 20.364 1.00 21.59 BBBB ATOM 4531 C VAL B 258 15.799 −26.585 − 17.389 1.00 19.70 BBBB ATOM 4532 O VAL B 258 16.808 −27.175 − 17.758 1.00 18.96 BBBB ATOM 4533 N VAL B 259 15.167 −26.861 − 16.253 1.00 20.24 BBBB ATOM 4534 CA VAL B 259 15.581 −27.957 − 15.374 1.00 19.85 BBBB ATOM 4535 CB VAL B 259 15.850 −27.483 − 13.936 1.00 20.08 BBBB ATOM 4536 CG1 VAL B 259 16.222 −28.689 − 13.059 1.00 20.22 BBBB ATOM 4537 CG2 VAL B 259 16.966 −26.453 − 13.930 1.00 17.86 BBBB ATOM 4538 C VAL B 259 14.382 −28.890 − 15.371 1.00 20.02 BBBB ATOM 4539 O VAL B 259 13.301 −28.500 − 14.942 1.00 21.88 BBBB ATOM 4540 N CYS B 260 14.562 −30.111 − 15.867 1.00 21.70 BBBB ATOM 4541 CA CYS B 260 13.454 −31.055 − 15.946 1.00 22.00 BBBB ATOM 4542 CB CYS B 260 12.494 −30.618 − 17.057 1.00 22.77 BBBB ATOM 4543 SC CYS B 260 13.297 −30.506 − 18.711 1.00 22.15 BBBB ATOM 4544 C CYS B 260 13.903 −32.478 − 16.242 1.00 21.86 BBBB ATOM 4545 O CYS B 260 15.087 −32.730 − 16.496 1.00 21.34 BBBB ATOM 4546 N ARG B 261 12.937 −33.397 − 16.212 1.00 22.34 BBBB ATOM 4547 CA ARG B 261 13.170 −34.800 − 16.515 1.00 23.75 BBBB ATOM 4548 CB ARG B 261 11.964 −35.663 − 16.104 1.00 27.16 BBBB ATOM 4549 CG ARG B 261 11.376 −35.337 − 14.738 1.00 31.82 BBBB ATOM 4550 CD ARG B 261 11.490 −36.473 − 13.732 1.00 36.33 BBBB ATOM 4551 NE ARG B 261 12.865 −36.721 − 13.323 1.00 38.48 BBBB ATOM 4552 CZ ARG B 261 13.218 −37.176 − 12.125 1.00 37.25 BBBB ATOM 4553 NB1 ARG B 261 12.295 −37.433 − 11.204 1.00 38.46 BBBB ATOM 4554 NH2 ARG B 261 14.499 −37.370 − 11.848 1.00 36.79 BBBB ATOM 4555 C ARG B 261 13.351 −34.871 − 18.032 1.00 23.98 BBBB ATOM 4556 O ARG B 261 13.117 −33.883 − 18.746 1.00 22.44 BBBB ATOM 4557 N SER B 262 13.740 −36.038 − 18.527 1.00 22.00 BBBB ATOM 4558 CA SER B 262 13.975 −36.189 − 19.948 1.00 23.18 BBBB ATOM 4559 CB SER B 262 15.481 −36.377 − 20.203 1.00 24.45 BBBB ATOM 4560 OG SER B 262 16.043 −37.326 − 19.311 1.00 25.79 BBBB ATOM 4561 C SER B 262 13.173 −37.263 − 20.676 1.00 22.90 BBBB ATOM 4562 O SER B 262 13.738 −38.179 −21.274 1.00 23.25 BBBB ATOM 4563 N GLY B 263 11.850 −37.151 − 20.619 1.00 22.74 BBBB ATOM 4564 CA GLY B 263 11.026 −38.079 −21.361 1.00 22.85 BBBB ATOM 4565 C GLY B 263 11.392 −37.793 −22.813 1.00 24.06 BBBB ATOM 4566 O GLY B 263 11.908 −36.705 −23.121 1.00 22.75 BBBB ATOM 4567 N ALA B 264 11.130 −38.739 −23.708 1.00 23.37 BBBB ATOM 4568 CA ALA B 264 11.482 −38.564 −25.115 1.00 24.25 BBBB ATOM 4569 CB ALA B 264 11.133 −39.829 −25.894 1.00 24.58 BBBB ATOM 4570 C ALA B 264 10.843 −37.343 −25.783 1.00 24.29 BBBB ATOM 4571 O ALA B 264 11.523 −36.572 −26.470 1.00 24.33 BBBB ATOM 4572 N LEU B 265 9.541 −37.167 −25.596 1.00 24.44 BBBB ATOM 4573 CA LEU B 265 8.846 −36.037 −26.205 1.00 24.66 BBBB ATOM 4574 CB LEU B 265 7.332 −36.183 −26.011 1.00 25.33 BBBB ATOM 4575 CG LEU B 265 6.760 −37.544 −26.426 1.00 27.97 BBBB ATOM 4576 CD1 LEU B 265 5.242 −37.541 −26.258 1.00 28.21 BBBB ATOM 4577 CD2 LEU B 265 7.146 −37.856 −27.878 1.00 27.40 BBBB ATOM 4578 C LEU B 265 9.331 −34.717 −25.613 1.00 24.47 BBBB ATOM 4579 O LEU B 265 9.374 −33.693 −26.301 1.00 23.85 BBBB ATOM 4580 N THR B 266 9.702 −34.747 −24.338 1.00 22.12 BBBB ATOM 4581 CA THR B 266 10.194 −33.557 −23.657 1.00 22.34 BBBB ATOM 4582 CB THR B 266 10.348 −33.803 −22.140 1.00 22.35 BBBB ATOM 4583 OE1 THR B 266 9.061 −34.087 −21.583 1.00 24.46 BBBB ATOM 4584 CG2 THR B 266 10.945 −32.573 −21.444 1.00 24.00 BBBB ATOM 4585 C THR B 266 11.535 −33.117 −24.226 1.00 21.15 BBBB ATOM 4586 O THR B 266 11.761 −31.926 −24.442 1.00 20.35 BBBB ATOM 4587 N VAL B 267 12.427 −34.075 −24.461 1.00 20.46 BBBB ATOM 4588 CA VAL B 267 13.730 −33.762 −25.023 1.00 21.11 BBBB ATOM 4589 CB VAL B 267 14.614 −35.039 −25.114 1.00 21.54 BBBB ATOM 4590 CG1 VAL B 267 15.903 −34.740 −25.865 1.00 20.72 BBBB ATOM 4591 CG2 VAL B 267 14.938 −35.541 −23.708 1.00 20.45 BBBB ATOM 4592 C VAL B 267 13.548 −33.138 −26.416 1.00 21.34 BBBB ATOM 4593 O VAL B 267 14.188 −32.135 −26.747 1.00 19.99 BBBB ATOM 4594 N SER B 268 12.663 −33.717 −27.222 1.00 21.61 BBBB ATOM 4595 CA SER B 268 12.411 −33.191 −28.567 1.00 21.96 BBBB ATOM 4596 CB SER B 268 11.474 −34.121 −29.344 1.00 21.57 BBBB ATOM 4597 OG SER B 268 12.141 −35.316 −29.721 1.00 24.06 BBBB ATOM 4598 C SER B 268 11.817 −31.790 −28.519 1.00 21.81 BBBB ATOM 4599 O SER B 268 12.158 −30.933 −29.336 1.00 22.60 BBBB ATOM 4600 N GLU B 269 10.928 −31.563 −27.557 1.00 21.64 BBBB ATOM 4601 CA GLU B 269 10.282 −30.272 −27.378 1.00 21.95 BBBB ATOM 4602 CB GLU B 269 9.213 −30.399 −26.292 1.00 24.72 BBBB ATOM 4603 CG GLU B 269 8.480 −29.128 −25.940 1.00 27.67 BBBB ATOM 4604 CD GLU B 269 7.385 −29.380 −24.908 1.00 30.05 BBBB ATOM 4605 OE1 GLU B 269 6.325 −29.915 −25.287 1.00 31.50 BBBB ATOM 4606 OE2 GLU B 269 7.591 −29.057 −23.719 1.00 29.84 BBBB ATOM 4607 C GLU B 269 11.321 −29.214 −26.999 1.00 21.68 BBBB ATOM 4608 O GLU B 269 11.301 −28.095 −27.518 1.00 18.12 BBBB ATOM 4609 N ILE B 270 12.224 −29.581 −26.092 1.00 19.43 BBBB ATOM 4610 CA ILE B 270 13.295 −28.698 −25.638 1.00 20.62 BBBB ATOM 4611 CB ILE B 270 14.157 −29.391 −24.533 1.00 20.30 BBBB ATOM 4612 CG2 ILE B 270 15.415 −28.595 −24.266 1.00 19.17 BBBB ATOM 4613 CG1 ILE B 270 13.337 −29.574 −23.254 1.00 21.32 BBBB ATOM 4614 CD1 ILE B 270 12.926 −28.291 −22.583 1.00 23.40 BBBB ATOM 4615 C ILE B 270 14.214 −28.314 −26.806 1.00 20.58 BBBB ATOM 4616 O ILE B 270 14.595 −27.151 −26.954 1.00 20.50 BBBB ATOM 4617 N ALA B 271 14.574 −29.298 −27.624 1.00 21.29 BBBB ATOM 4618 CA ALA B 271 15.440 −29.058 −28.776 1.00 22.45 BBBB ATOM 4619 CB ALA B 271 15.741 −30.376 −29.485 1.00 23.36 BBBB ATOM 4620 C ALA B 271 14.766 −28.084 −29.745 1.00 23.03 BBBB ATOM 4621 O ALA B 271 15.400 −27.156 −30.259 1.00 23.57 BBBB ATOM 4622 N ALA B 272 13.479 −28.301 −29.988 1.00 21.81 BBBB ATOM 4623 CA ALA B 272 12.719 −27.451 −30.898 1.00 22.17 BBBB ATOM 4624 CB ALA B 272 11.335 −28.053 −31.131 1.00 22.15 BBBB ATOM 4625 C ALA B 272 12.590 −26.030 −30.355 1.00 22.78 BBBB ATOM 4626 O ALA B 272 12.585 −25.058 −31.122 1.00 21.77 BBBB ATOM 4627 N ALA B 273 12.474 −25.907 −29.034 1.00 21.06 BBBB ATOM 4628 CA ALA B 273 12.361 −24.596 −28.407 1.00 21.97 BBBB ATOM 4629 CB ALA B 273 11.919 −24.737 −26.949 1.00 20.63 BBBB ATOM 4630 C ALA B 273 13.699 −23.867 −28.468 1.00 21.83 BBBB ATOM 4631 O ALA B 273 13.754 −22.642 −28.344 1.00 22.67 BBBB ATOM 4632 N GLY B 274 14.773 −24.621 −28.656 1.00 20.90 BBBB ATOM 4633 CA GLY B 274 16.093 −24.023 −28.709 1.00 21.07 BBBB ATOM 4634 C GLY B 274 16.498 −23.549 −27.327 1.00 21.48 BBBB ATOM 4635 O GLY B 274 16.961 −22.421 −27.154 1.00 20.01 BBBB ATOM 4636 N LEU B 275 16.331 −24.420 −26.333 1.00 19.66 BBBB ATOM 4637 CA LEU B 275 16.666 −24.057 −24.966 1.00 19.78 BBBB ATOM 4638 CB LEU B 275 15.402 −24.068 −24.102 1.00 21.30 BBBB ATOM 4639 CG LEU B 275 14.451 −22.870 −24.202 1.00 24.60 BBBB ATOM 4640 CD1 LEU B 275 13.220 −23.136 −23.349 1.00 26.44 BBBB ATOM 4641 CD2 LEU B 275 15.159 −21.609 −23.725 1.00 24.02 BBBB ATOM 4642 C LEU B 275 17.698 −24.970 −24.318 1.00 18.79 BBBB ATOM 4643 O LEU B 275 17.679 −26.180 −24.524 1.00 19.36 BBBB ATOM 4644 N PRO B 276 18.634 −24.389 −23.554 1.00 17.27 BBBB ATOM 4645 CD PRO B 276 18.925 −22.955 −23.416 1.00 16.95 BBBB ATOM 4646 CA PRO B 276 19.651 −25.199 −22.875 1.00 16.62 BBBB ATOM 4647 CB PRO B 276 20.619 −24.162 −22.317 1.00 17.27 BBBB ATOM 4648 CG PRO B 276 20.408 −22.957 −23.195 1.00 18.59 BBBB ATOM 4649 C PRO B 276 18.900 −25.900 −21.746 1.00 17.23 BBBB ATOM 4650 O PRO B 276 17.944 −25.340 −21.189 1.00 15.14 BBBB ATOM 4651 N ALA B 277 19.316 −27.110 −21.396 1.00 17.01 BBBB ATOM 4652 CA ALA B 277 18.638 −27.807 − 20.321 1.00 15.80 BBBB ATOM 4653 CB ALA B 277 17.641 −28.805 − 20.895 1.00 17.01 BBBB ATOM 4654 C ALA B 277 19.591 −28.526 − 19.382 1.00 17.37 BBBB ATOM 4655 O ALA B 277 20.710 −28.891 − 19.755 1.00 17.09 BBBB ATOM 4656 N LEU B 278 19.147 −28.673 − 18.138 1.00 17.14 BBBB ATOM 4657 CA LEU B 278 19.896 −29.429 − 17.145 1.00 18.48 BBBB ATOM 4658 CB LEU B 278 20.140 −28.619 − 15.869 1.00 19.19 BBBB ATOM 4659 CG LEU B 278 21.084 −29.308 − 14.868 1.00 20.85 BBBB ATOM 4660 CD1 LEU B 278 21.283 −28.411 − 13.668 1.00 21.11 BBBB ATOM 4661 CD2 LEU B 278 20.497 −30.647 − 14.433 1.00 19.16 BBBB ATOM 4662 C LEU B 278 18.884 −30.535 − 16.898 1.00 19.62 BBBB ATOM 4663 O LEU B 278 17.870 −30.330 − 16.218 1.00 20.77 BBBB ATOM 4664 N PHE B 279 19.149 −31.691 − 17.495 1.00 19.50 BBBB ATOM 4665 CA PHE B 279 18.266 −32.838 − 17.392 1.00 21.59 BBBB ATOM 4666 CB PHE B 279 18.385 −33.700 − 18.651 1.00 21.07 BBBB ATOM 4667 CG PHE B 279 17.740 −33.099 − 19.876 1.00 19.35 BBBB ATOM 4668 CD1 PHE B 279 18.481 −32.898 −21.035 1.00 19.42 BBBB ATOM 4669 CD2 PHE B 279 16.379 −32.794 − 19.888 1.00 18.16 BBBB ATOM 4670 CE1 PHE B 279 17.874 −32.405 −22.203 1.00 19.06 BBBB ATOM 4671 CE2 PHE B 279 15.759 −32.298 −21.052 1.00 17.65 BBBB ATOM 4672 CZ PHE B 279 16.515 −32.108 −22.208 1.00 15.61 BBBB ATOM 4673 C PHE B 279 18.525 −33.709 − 16.167 1.00 22.86 BBBB ATOM 4674 O PHE B 279 19.671 −34.065 − 15.871 1.00 23.32 BBBB ATOM 4675 N VAL B 280 17.445 −34.037 − 15.461 1.00 23.88 BBBB ATOM 4676 CA VAL B 280 17.502 −34.902 − 14.281 1.00 25.67 BBBB ATOM 4677 CB VAL B 280 16.883 −34.223 − 13.048 1.00 26.89 BBBB ATOM 4678 CG1 VAL B 280 16.954 −35.159 − 11.847 1.00 28.12 BBBB ATOM 4679 CG2 VAL B 280 17.631 −32.929 − 12.742 1.00 27.70 BBBB ATOM 4680 C VAL B 280 16.690 −36.136 − 14.658 1.00 25.65 BBBB ATOM 4681 O VAL B 280 15.509 −36.239 − 14.346 1.00 24.57 BBBB ATOM 4682 N PRO B 281 17.324 −37.080 − 15.370 1.00 27.08 BBBB ATOM 4683 CD PRO B 281 18.750 −37.057 − 15.726 1.00 27.31 BBBB ATOM 4684 CA PRO B 281 16.698 −38.320 − 15.824 1.00 29.05 BBBB ATOM 4685 CB PRO B 281 17.851 −39.071 − 16.492 1.00 29.44 BBBB ATOM 4686 CG PRO B 281 18.791 −37.992 − 16.895 1.00 29.67 BBBB ATOM 4687 C PRO B 281 16.092 −39.121 − 14.684 1.00 31.51 BBBB ATOM 4688 O PRO B 281 16.675 −39.223 − 13.603 1.00 32.26 BBBB ATOM 4689 N PHE B 282 14.908 −39.668 − 14.923 1.00 33.83 BBBB ATOM 4690 CA PHE B 282 14.246 −40.496 − 13.926 1.00 37.13 BBBB ATOM 4691 CB PHE B 282 12.818 −40.808 − 14.372 1.00 38.38 BBBB ATOM 4692 CG PHE B 282 12.032 −41.606 − 13.377 1.00 40.57 BBBB ATOM 4693 CD1 PHE B 282 11.720 −41.074 − 12.130 1.00 41.80 BBBB ATOM 4694 CD2 PHE B 282 11.590 −42.886 − 13.689 1.00 41.65 BBBB ATOM 4695 CE1 PHE B 282 10.975 −41.806 − 11.209 1.00 42.03 BBBB ATOM 4696 CE2 PHE B 282 10.843 −43.628 − 12.773 1.00 42.49 BBBB ATOM 4697 CZ PHE B 282 10.536 −43.085 − 11.532 1.00 41.74 BBBB ATOM 4698 C PHE B 282 15.078 −41.776 − 13.880 1.00 38.09 BBBB ATOM 4699 O PHE B 282 15.357 −42.373 − 14.921 1.00 38.33 BBBB ATOM 4700 N GLN B 283 15.492 −42.197 − 12.690 1.00 39.70 BBBB ATOM 4701 CA GLN B 283 16.319 −43.395 − 12.591 1.00 41.11 BBBB ATOM 4702 CB GLN B 283 17.010 −43.477 − 11.223 1.00 41.41 BBBB ATOM 4703 CG GLN B 283 17.953 −44.676 − 11.096 1.00 42.60 BBBB ATOM 4704 CD GLN B 283 19.143 −44.605 − 12.051 1.00 42.87 BBBB ATOM 4705 OE1 GLN B 283 20.199 −44.068 − 11.712 1.00 43.66 BBBB ATOM 4706 NE2 GLN B 283 18.969 −45.135 − 13.254 1.00 42.46 BBBB ATOM 4707 C GLN B 283 15.543 −44.679 − 12.846 1.00 41.60 BBBB ATOM 4708 O GLN B 283 14.382 −44.809 − 12.462 1.00 40.91 BBBB ATOM 4709 N HIS B 284 16.211 −45.618 − 13.511 1.00 42.92 BBBB ATOM 4710 CA HIS B 284 15.641 −46.917 − 13.843 1.00 43.69 BBBB ATOM 4711 CB HIS B 284 14.508 −46.760 − 14.858 1.00 43.91 BBBB ATOM 4712 CG HIS B 284 13.795 −48.039 − 15.165 1.00 44.71 BBBB ATOM 4713 CD2 HIS B 284 12.574 −48.489 − 14.793 1.00 44.80 BBBB ATOM 4714 ND1 HIS B 284 14.360 −49.044 − 15.923 1.00 44.69 BBBB ATOM 4715 CE1 HIS B 284 13.516 −50.058 − 16.002 1.00 45.06 BBBB ATOM 4716 NE2 HIS B 284 12.425 −49.747 − 15.325 1.00 44.90 BBBB ATOM 4717 C HIS B 284 16.749 −47.788 − 14.424 1.00 44.09 BBBB ATOM 4718 O HIS B 284 17.602 −47.302 − 15.164 1.00 43.02 BBBB ATOM 4719 N LYS B 285 16.740 −49.074 − 14.085 1.00 44.90 BBBB ATOM 4720 CA LYS B 285 17.767 −49.993 − 14.571 1.00 45.34 BBBB ATOM 4721 CB LYS B 285 17.386 −51.436 − 14.222 1.00 46.84 BBBB ATOM 4722 CG LYS B 285 18.541 −52.425 − 14.327 1.00 49.53 BBBB ATOM 4723 CD LYS B 285 18.140 −53.802 − 13.807 1.00 51.08 BBBB ATOM 4724 CE LYS B 285 19.325 −54.759 − 13.780 1.00 51.58 BBBB ATOM 4725 NZ LYS B 285 18.931 −56.115 − 13.292 1.00 52.11 BBBB ATOM 4726 C LYS B 285 17.969 −49.853 − 16.079 1.00 45.02 BBBB ATOM 4727 O LYS B 285 19.067 −50.070 − 16.595 1.00 45.49 BBBB ATOM 4728 N ASP B 286 16.903 −49.478 − 16.777 1.00 44.33 BBBB ATOM 4729 CA ASP B 286 16.949 −49.299 − 18.222 1.00 43.26 BBBB ATOM 4730 CB ASP B 286 15.532 −49.379 − 18.794 1.00 45.91 BBBB ATOM 4731 CG ASP B 286 15.511 −49.354 − 20.304 1.00 48.32 BBBB ATOM 4732 OD1 ASP B 286 15.971 −50.338 − 20.925 1.00 49.52 BBBB ATOM 4733 OD2 ASP B 286 15.037 −48.346 − 20.872 1.00 51.04 BBBB ATOM 4734 C ASP B 286 17.573 −47.947 − 18.582 1.00 40.92 BBBB ATOM 4735 O ASP B 286 18.179 −47.796 − 19.643 1.00 40.31 BBBB ATOM 4736 N ARG B 287 17.415 −46.972 − 17.689 1.00 38.60 BBBB ATOM 4737 CA ARG B 287 17.951 −45.623 − 17.883 1.00 36.28 BBBB ATOM 4738 CB ARG B 287 19.477 −45.650 − 17.910 1.00 37.28 BBBB ATOM 4739 CG ARG B 287 20.116 −46.263 − 16.687 1.00 40.54 BBBB ATOM 4740 CD ARG B 287 21.605 −46.395 − 16.906 1.00 42.34 BBBB ATOM 4741 NE ARG B 287 22.291 −45.113 − 16.802 1.00 44.33 BBBB ATOM 4742 CZ ARG B 287 23.449 −44.842 − 17.392 1.00 45.20 BBBB ATOM 4743 NH1 ARG B 287 24.045 −45.764 − 18.135 1.00 45.60 BBBB ATOM 4744 NH2 ARG B 287 24.019 −43.656 − 17.227 1.00 45.68 BBBB ATOM 4745 C ARG B 287 17.449 −45.005 − 19.180 1.00 33.59 BBBB ATOM 4746 O ARG B 287 18.167 −44.255 − 19.844 1.00 32.61 BBBB ATOM 4747 N GLN B 288 16.212 −45.321 − 19.533 1.00 30.94 BBBB ATOM 4748 CA GLN B 288 15.622 −44.804 − 20.755 1.00 30.77 BBBB ATOM 4749 CB GLN B 288 14.143 −45.158 − 20.810 1.00 30.59 BBBB ATOM 4750 CG GLN B 288 13.473 −44.772 −22.109 1.00 29.73 BBBB ATOM 4751 CD GLN B 288 11.981 −44.971 −22.044 1.00 28.04 BBBB ATOM 4752 OE1 GLN B 288 11.294 −44.295 −21.279 1.00 29.59 BBBB ATOM 4753 NE2 GLN B 288 11.468 −45.905 −22.838 1.00 26.98 BBBB ATOM 4754 C GLN B 288 15.783 −43.291 − 20.885 1.00 29.70 BBBB ATOM 4755 O GLN B 288 16.268 −42.801 −21.902 1.00 29.79 BBBB ATOM 4756 N GLN B 289 15.378 −42.554 − 19.857 1.00 29.38 BBBB ATOM 4757 CA GLN B 289 15.474 −41.099 − 19.904 1.00 29.46 HBBH ATOM 4758 CB GLN B 289 14.772 −40.472 − 18.700 1.00 29.25 BBBB ATOM 4759 CG GLN B 289 13.265 −40.416 − 18.883 1.00 29.32 BBBB ATOM 4760 CD GLN B 289 12.575 −39.585 − 17.826 1.00 29.84 BBBB ATOM 4761 OE1 GLN B 289 13.191 −38.728 − 17.188 1.00 29.52 BBBB ATOM 4762 NE2 GLN B 289 11.281 −39.821 − 17.647 1.00 28.95 BBBB ATOM 4763 C GLN B 289 16.906 −40.613 − 20.005 1.00 29.36 BBBB ATOM 4764 O GLN B 289 17.173 −39.557 − 20.585 1.00 29.12 BBBB ATOM 4765 N TYR B 290 17.835 −41.374 − 19.442 1.00 28.95 BBBB ATOM 4766 CA TYR B 290 19.228 −40.984 − 19.550 1.00 29.55 BBBB ATOM 4767 CB TYR B 290 20.136 −41.934 − 18.768 1.00 31.40 BBBB ATOM 4768 CG TYR B 290 21.587 −41.780 − 19.148 1.00 33.37 BBBB ATOM 4769 CD1 TYR B 290 22.332 −40.682 − 18.717 1.00 34.57 BBBB ATOM 4770 CE1 TYR B 290 23.644 −40.490 − 19.148 1.00 35.97 BBBB ATOM 4771 CD2 TYR B 290 22.192 −42.684 − 20.017 1.00 34.90 BBBB ATOM 4772 CE2 TYR B 290 23.497 −42.500 − 20.453 1.00 36.03 BBBB ATOM 4773 CZ TYR B 290 24.214 −41.402 − 20.019 1.00 36.29 BBBB ATOM 4774 OH TYR B 290 25.499 −41.215 − 20.475 1.00 39.44 BBBB ATOM 4775 C TYR B 290 19.593 −41.042 −21.032 1.00 28.80 BBBB ATOM 4776 O TYR B 290 20.192 −40.113 −21.567 1.00 29.22 BBBB ATOM 4777 N TRP B 291 19.227 −42.135 −21.697 1.00 27.57 BBBB ATOM 4778 CA TRP B 291 19.542 −42.282 −23.116 1.00 28.07 BBBB ATOM 4779 CB TRP B 291 19.217 −43.705 −23.599 1.00 29.42 BBBB ATOM 4780 CG TRP B 291 20.070 −44.750 −22.936 1.00 31.82 BBBB ATOM 4781 CD2 TRP B 291 21.487 −44.908 −23.069 1.00 33.22 BBBB ATOM 4782 CE2 TRP B 291 21.873 −45.966 −22.213 1.00 33.81 BBBB ATOM 4783 CE3 TRP B 291 22.470 −44.257 −23.826 1.00 33.13 BBBB ATOM 4784 CD1 TRP B 291 19.663 −45.695 −22.035 1.00 32.62 BBBB ATOM 4785 NE1 TRP B 291 20.741 −46.428 −21.595 1.00 33.43 BBBB ATOM 4786 CZ2 TRP B 291 23.203 −46.387 −22.093 1.00 34.69 BBBB ATOM 4787 CZ3 TRP B 291 23.794 −44.676 −23.707 1.00 35.41 BBBB ATOM 4788 CH2 TRP B 291 24.146 −45.732 −22.845 1.00 35.26 BBBB ATOM 4789 C TRP B 291 18.808 −41.256 −23.978 1.00 26.84 BBBB ATOM 4790 O TRP B 291 19.283 −40.900 −25.058 1.00 26.55 BBBB ATOM 4791 N ASN B 292 17.658 −40.779 −23.508 1.00 25.52 BBBB ATOM 4792 CA ASN B 292 16.902 −39.784 −24.270 1.00 26.06 BBBB ATOM 4793 CB ASN B 292 15.484 −39.599 −23.709 1.00 24.78 BBBB ATOM 4794 CG ASN B 292 14.590 −40.811 −23.928 1.00 24.46 BBBB ATOM 4795 OD1 ASN B 292 14.842 −41.641 −24.798 1.00 25.33 BBBB ATOM 4796 ND2 ASN B 292 13.523 −40.900 −23.146 1.00 23.83 BBBB ATOM 4797 C ASN B 292 17.605 −38.427 −24.258 1.00 25.99 BBBB ATOM 4798 O ASN B 292 17.566 −37.687 −25.244 1.00 26.18 BBBB ATOM 4799 N ALA B 293 18.242 −38.105 −23.139 1.00 25.66 BBBB ATOM 4800 CA ALA B 293 18.926 −36.822 −22.979 1.00 25.69 BBBB ATOM 4801 CB ALA B 293 18.940 −36.422 −21.506 1.00 24.17 BBBB ATOM 4802 C ALA B 293 20.346 −36.800 −23.521 1.00 25.67 BBBB ATOM 4803 O ALA B 293 20.855 −35.743 −23.902 1.00 25.52 BBBB ATOM 4804 N LEU B 294 20.978 −37.969 −23.560 1.00 25.62 BBBB ATOM 4805 CA LEU B 294 22.354 −38.088 −24.032 1.00 25.90 BBBB ATOM 4806 CB LEU B 294 22.745 −39.566 −24.121 1.00 26.51 BBBB ATOM 4807 CG LEU B 294 24.226 −39.864 −24.350 1.00 28.12 BBBB ATOM 4808 CD1 LEU B 294 25.085 −39.055 −23.380 1.00 28.29 BBBB ATOM 4809 CD2 LEU B 294 24.470 −41.368 −24.169 1.00 28.15 BBBB ATOM 4810 C LEU B 294 22.644 −37.392 −25.359 1.00 25.66 BBBB ATOM 4811 O LEU B 294 23.677 −36.741 −25.507 1.00 24.79 BBBB ATOM 4812 N PRO B 295 21.748 −37.532 −26.351 1.00 26.24 BBBB ATOM 4813 CD PRO B 295 20.560 −38.400 −26.437 1.00 25.75 BBBB ATOM 4814 CA PRO B 295 21.998 −36.870 −27.635 1.00 26.15 BBBB ATOM 4815 CB PRO B 295 20.740 −37.201 −28.439 1.00 26.70 BBBB ATOM 4816 CG PRO B 295 20.382 −38.548 −27.932 1.00 26.84 BBBB ATOM 4817 C PRO B 295 22.219 −35.358 −27.480 1.00 25.78 BBBB ATOM 4818 O PRO B 295 23.138 −34.792 −28.069 1.00 25.05 BBBB ATOM 4819 N LEU B 296 21.375 −34.703 −26.688 1.00 25.66 BBBB ATOM 4820 CA LEU B 296 21.521 −33.265 −26.481 1.00 25.42 BBBB ATOM 4821 CB LEU B 296 20.283 −32.685 −25.779 1.00 24.45 BBBB ATOM 4822 CG LEU B 296 19.066 −32.458 −26.679 1.00 25.59 BBBB ATOM 4823 CD1 LEU B 296 17.968 −31.718 −25.911 1.00 23.56 BBBB ATOM 4824 CD2 LEU B 296 19.496 −31.630 −27.893 1.00 25.87 BBBB ATOM 4825 C LEU B 296 22.784 −32.935 −25.688 1.00 26.07 BBBB ATOM 4826 O LEU B 296 23.435 −31.917 −25.944 1.00 25.26 BBBB ATOM 4827 N GLU B 297 23.143 −33.785 −24.730 1.00 26.14 BBBB ATOM 4828 CA GLU B 297 24.354 −33.530 −23.953 1.00 28.78 BBBB ATOM 4829 CB GLU B 297 24.470 −34.483 −22.755 1.00 29.05 BBBB ATOM 4830 CG GLU B 297 25.716 −34.210 −21.908 1.00 30.81 BBBB ATOM 4831 CD GLU B 297 25.812 −35.087 − 20.671 1.00 31.84 BBBB ATOM 4832 OE1 GLU B 297 25.655 −34.555 − 19.551 1.00 31.74 BBBB ATOM 4833 OE2 GLU B 297 26.045 −36.307 − 20.820 1.00 31.56 BBBB ATOM 4834 C GLU B 297 25.577 −33.686 −24.846 1.00 29.06 BBBB ATOM 4835 O GLU B 297 26.528 −32.910 −24.746 1.00 29.11 BBBB ATOM 4836 N LYS B 298 25.543 −34.688 −25.722 1.00 31.21 BBBB ATOM 4837 CA LYS B 298 26.644 −34.947 −26.648 1.00 31.90 BBBB ATOM 4838 CB LYS B 298 26.379 −36.216 −27.464 1.00 33.65 BBBB ATOM 4839 CG LYS B 298 26.519 −37.514 −26.680 1.00 36.05 BBBB ATOM 4840 CD LYS B 298 26.251 −38.734 −27.568 1.00 37.69 BBBB ATOM 4841 CE LYS B 298 26.461 −40.033 −26.801 1.00 38.51 BBBB ATOM 4842 NZ LYS B 298 26.094 −41.235 −27.607 1.00 39.05 BBBB ATOM 4843 C LYS B 298 26.829 −33.768 −27.598 1.00 31.69 BBBB ATOM 4844 O LYS B 298 27.945 −33.455 −27.998 1.00 30.87 BBBB ATOM 4845 N ALA B 299 25.725 −33.116 −27.952 1.00 31.63 BBBB ATOM 4846 CA ALA B 299 25.773 −31.965 −28.847 1.00 30.38 BBBB ATOM 4847 CB ALA B 299 24.415 −31.778 −29.521 1.00 30.22 BBBB ATOM 4848 C ALA B 299 26.173 −30.685 −28.106 1.00 29.94 BBBB ATOM 4849 O ALA B 299 26.278 −29.615 −28.709 1.00 30.96 BBBB ATOM 4850 N GLY B 300 26.398 −30.796 −26.801 1.00 27.41 BBBB ATOM 4851 CA GLY B 300 26.777 −29.635 −26.017 1.00 26.18 BBBB ATOM 4852 C GLY B 300 25.619 −28.665 −25.810 1.00 25.19 BBBB ATOM 4853 O GLY B 300 25.832 −27.466 −25.644 1.00 24.70 BBBB ATOM 4854 N ALA B 301 24.392 −29.179 −25.820 1.00 23.51 BBBB ATOM 4855 CA ALA B 301 23.214 −28.333 −25.638 1.00 22.50 BBBB ATOM 4856 CB ALA B 301 22.174 −28.644 −26.717 1.00 23.44 BBBB ATOM 4857 C ALA B 301 22.591 −28.510 −24.254 1.00 22.09 BBBB ATOM 4858 O ALA B 301 21.705 −27.746 −23.863 1.00 19.90 BBBB ATOM 4859 N ALA B 302 23.066 −29.504 −23.507 1.00 20.94 BBBB ATOM 4860 CA ALA B 302 22.516 −29.770 −22.186 1.00 21.78 BBBB ATOM 4861 CB ALA B 302 21.243 −30.595 −22.327 1.00 20.10 BBBB ATOM 4862 C ALA B 302 23.503 −30.507 −21.288 1.00 22.69 BBBB ATOM 4863 O ALA B 302 24.561 −30.948 −21.739 1.00 22.25 BBBB ATOM 4864 N LYS B 303 23.156 −30.613 − 20.009 1.00 24.62 BBBB ATOM 4865 CA LYS B 303 23.979 −31.340 − 19.048 1.00 25.86 BBBB ATOM 4866 CB LYS B 303 24.632 −30.401 − 18.036 1.00 27.85 BBBB ATOM 4867 CG LYS B 303 25.466 −31.146 − 16.986 1.00 29.37 BBBB ATOM 4868 CD LYS B 303 26.150 −30.186 − 16.025 1.00 32.41 BBBB ATOM 4869 CE LYS B 303 27.083 −30.912 − 15.056 1.00 33.22 BBBB ATOM 4870 NZ LYS B 303 27.827 −29.952 − 14.181 1.00 33.62 BBBB ATOM 4871 C LYS B 303 23.083 −32.319 − 18.302 1.00 26.41 BBBB ATOM 4872 O LYS B 303 22.015 −31.948 − 17.802 1.00 25.76 BBBB ATOM 4873 N ILE B 304 23.520 −33.570 − 18.234 1.00 25.65 BBBB ATOM 4874 CA ILE B 304 22.753 −34.598 − 17.550 1.00 27.17 BBBB ATOM 4875 CB ILE B 304 22.786 −35.946 − 18.316 1.00 27.06 BBBB ATOM 4876 CG2 ILE B 304 21.977 −36.996 − 17.555 1.00 28.49 BBBB ATOM 4877 CG1 ILE B 304 22.242 −35.769 − 19.733 1.00 27.61 BBBB ATOM 4878 CD1 ILE B 304 22.380 −37.009 − 20.599 1.00 27.05 BBBB ATOM 4879 C ILE B 304 23.308 −34.855 − 16.160 1.00 27.00 BBBB ATOM 4880 O ILE B 304 24.511 −35.012 − 15.986 1.00 27.46 BBBB ATOM 4881 N ILE B 305 22.428 −34.869 − 15.168 1.00 27.22 BBBB ATOM 4882 CA ILE B 305 22.843 −35.178 − 13.813 1.00 29.01 BBBB ATOM 4883 CB ILE B 305 22.713 −33.977 − 12.858 1.00 28.91 BBBB ATOM 4884 CG2 ILE B 305 23.063 −34.416 − 11.432 1.00 30.98 BBBB ATOM 4885 CG1 ILE B 305 23.660 −32.855 − 13.299 1.00 29.51 BBBB ATOM 4886 CD1 ILE B 305 23.674 −31.653 − 12.367 1.00 29.43 BBBB ATOM 4887 C ILE B 305 21.934 −36.302 − 13.351 1.00 29.64 BBBB ATOM 4888 O ILE B 305 20.806 −36.067 − 12.932 1.00 29.25 BBBB ATOM 4889 N GLU B 306 22.429 −37.532 − 13.467 1.00 32.18 BBBB ATOM 4890 CA GLU B 306 21.664 −38.702 − 13.061 1.00 34.65 BBBB ATOM 4891 CB GLU B 306 22.356 −39.989 − 13.530 1.00 34.79 BBBB ATOM 4892 CG GLU B 306 22.529 −40.067 − 15.035 1.00 36.39 BBBB ATOM 4893 CD GLU B 306 23.114 −41.388 − 15.504 1.00 36.86 BBBB ATOM 4894 OE1 GLU B 306 22.468 −42.433 − 15.289 1.00 36.59 BBBB ATOM 4895 OE2 GLU B 306 24.214 −41.378 − 16.099 1.00 37.75 BBBB ATOM 4896 C GLU B 306 21.531 −38.704 − 11.552 1.00 35.50 BBBB ATOM 4897 O GLU B 306 22.241 −37.984 − 10.858 1.00 35.55 BBBB ATOM 4898 N GLN B 307 20.612 −39.514 − 11.048 1.00 38.41 BBBB ATOM 4899 CA GLN B 307 20.377 −39.599 −9.613 1.00 40.54 BBBB ATOM 4900 CB GLN B 307 19.397 −40.734 −9.322 1.00 40.99 BBBB ATOM 4901 CG GLN B 307 18.896 −40.769 −7.896 1.00 42.76 BBBB ATOM 4902 CD GLN B 307 17.879 −41.867 −7.681 1.00 44.33 BBBB ATOM 4903 OE1 GLN B 307 18.181 −43.051 −7.847 1.00 44.46 BBBB ATOM 4904 NE2 GLN B 307 16.659 −41.481 −7.318 1.00 45.30 BBBB ATOM 4905 C GLN B 307 21.647 −39.784 −8.776 1.00 40.94 BBBB ATOM 4906 O GLN B 307 21.796 −39.154 −7.732 1.00 41.24 BBBB ATOM 4907 N PRO B 308 22.580 −40.648 −9.224 1.00 42.16 BBBB ATOM 4908 CD PRO B 308 22.456 −41.593 −10.349 1.00 42.40 BBBB ATOM 4909 CA PRO B 308 23.828 −40.891 −8.484 1.00 43.20 BBBB ATOM 4910 CB PRO B 308 24.533 −41.954 −9.329 1.00 43.16 BBBB ATOM 4911 CG PRO B 308 23.395 −42.708 −9.938 1.00 43.10 BBBB ATOM 4912 C PRO B 308 24.719 −39.668 −8.250 1.00 43.82 BBBB ATOM 4913 O PRO B 308 25.652 −39.724 −7.449 1.00 44.24 BBBB ATOM 4914 N GLN B 309 24.442 −38.569 −8.944 1.00 44.04 BBBB ATOM 4915 CA GLN B 309 25.247 −37.361 −8.787 1.00 43.46 BBBB ATOM 4916 CB GLN B 309 26.071 −37.104 − 10.056 1.00 44.98 BBBB ATOM 4917 CG GLN B 309 27.183 −38.113 − 10.329 1.00 46.93 BBBB ATOM 4918 CD GLN B 309 26.683 −39.437 − 10.885 1.00 47.93 BBBB ATOM 4919 OE1 GLN B 309 27.459 −40.376 − 11.054 1.00 48.87 BBBB ATOM 4920 NE2 GLN B 309 25.388 −39.515 − 11.179 1.00 49.17 BBBB ATOM 4921 C GLN B 309 24.417 −36.119 −8.479 1.00 42.87 BBBB ATOM 4922 O GLN B 309 24.955 −35.013 −8.404 1.00 43.33 BBBB ATOM 4923 N LEU B 310 23.113 −36.297 −8.289 1.00 41.06 BBBB ATOM 4924 CA LEU B 310 22.232 −35.166 −8.022 1.00 39.65 BBBB ATOM 4925 CB LEU B 310 20.779 −35.549 −8.330 1.00 39.95 BBBB ATOM 4926 CG LEU B 310 19.730 −34.437 −8.480 1.00 39.98 BBBB ATOM 4927 CD1 LEU B 310 19.545 −33.699 −7.166 1.00 41.39 BBBB ATOM 4928 CD2 LEU B 310 20.160 −33.472 −9.580 1.00 40.19 BBBB ATOM 4929 C LEU B 310 22.342 −34.659 −6.591 1.00 38.83 BBBB ATOM 4930 O LEU B 310 22.246 −35.428 −5.634 1.00 39.25 BBBB ATOM 4931 N SER B 311 22.541 −33.354 −6.457 1.00 36.17 BBBB ATOM 4932 CA SER B 311 22.660 −32.714 −5.154 1.00 34.90 BBBB ATOM 4933 CB SER B 311 24.059 −32.928 −4.569 1.00 35.08 BBBB ATOM 4934 OG SER B 311 25.022 −32.135 −5.248 1.00 33.92 BBBB ATOM 4935 C SER B 311 22.434 −31.227 −5.357 1.00 33.51 BBBB ATOM 4936 O SER B 311 22.476 −30.741 −6.485 1.00 33.60 BBBB ATOM 4937 N VAL B 312 22.202 −30.509 −4.266 1.00 32.42 BBBB ATOM 4938 CA VAL B 312 21.990 −29.074 −4.341 1.00 31.50 BBBB ATOM 4939 CB VAL B 312 21.707 −28.482 −2.938 1.00 31.69 BBBB ATOM 4940 CG1 VAL B 312 21.546 −26.976 −3.023 1.00 31.54 BBBB ATOM 4941 CG2 VAL B 312 20.445 −29.106 −2.362 1.00 31.93 BBBB ATOM 4942 C VAL B 312 23.228 −28.417 −4.946 1.00 31.40 BBBB ATOM 4943 O VAL B 312 23.123 −27.612 −5.875 1.00 30.04 BBBB ATOM 4944 N ASP B 313 24.406 −28.780 −4.444 1.00 30.18 BBBB ATOM 4945 CA ASP B 313 25.642 −28.202 −4.957 1.00 29.61 BBBB ATOM 4946 CB ASP B 313 26.840 −28.656 −4.120 1.00 32.36 BBBB ATOM 4947 CG ASP B 313 26.817 −28.085 −2.718 1.00 34.21 BBBB ATOM 4948 OD1 ASP B 313 26.662 −26.855 −2.578 1.00 36.52 BBBB ATOM 4949 OD2 ASP B 313 26.958 −28.865 −1.751 1.00 38.92 BBBB ATOM 4950 C ASP B 313 25.910 −28.516 −6.425 1.00 28.84 BBBB ATOM 4951 O ASP B 313 26.442 −27.677 −7.146 1.00 28.96 BBBB ATOM 4952 N ALA B 314 25.555 −29.719 −6.868 1.00 26.61 BBBB ATOM 4953 CA ALA B 314 25.782 −30.099 −8.254 1.00 26.47 BBBB ATOM 4954 CB ALA B 314 25.441 −31.575 −8.460 1.00 26.05 BBBB ATOM 4955 C ALA B 314 24.928 −29.220 −9.174 1.00 25.78 BBBB ATOM 4956 O ALA B 314 25.412 −28.714 − 10.187 1.00 24.94 BBBB ATOM 4957 N VAL B 315 23.661 −29.046 −8.815 1.00 25.00 BBBB ATOM 4958 CA VAL B 315 22.755 −28.215 −9.612 1.00 25.33 BBBB ATOM 4959 CB VAL B 315 21.305 −28.298 −9.088 1.00 24.74 BBBB ATOM 4960 CG1 VAL B 315 20.392 −27.382 −9.898 1.00 23.53 BBBB ATOM 4961 CG2 VAL B 315 20.810 −29.738 −9.172 1.00 25.69 BBBB ATOM 4962 C VAL B 315 23.222 −26.764 −9.561 1.00 25.02 BBBB ATOM 4963 O VAL B 315 23.398 −26.125 − 10.590 1.00 25.73 BBBB ATOM 4964 N ALA B 316 23.445 −26.251 −8.359 1.00 26.04 BBBB ATOM 4965 CA ALA B 316 23.888 −24.872 −8.199 1.00 27.13 BBBB ATOM 4966 CB ALA B 316 24.059 −24.545 −6.714 1.00 27.12 BBBB ATOM 4967 C ALA B 316 25.185 −24.584 −8.955 1.00 28.17 BBBB ATOM 4968 O ALA B 316 25.289 −23.572 −9.652 1.00 27.04 BBBB ATOM 4969 N ASN B 317 26.178 −25.463 −8.823 1.00 28.72 BBBB ATOM 4970 CA ASN B 317 27.444 −25.246 −9.518 1.00 28.52 BBBB ATOM 4971 CB ASN B 317 28.493 −26.271 −9.081 1.00 31.30 BBBB ATOM 4972 CG ASN B 317 28.940 −26.068 −7.645 1.00 34.01 BBBB ATOM 4973 OD1 ASN B 317 29.091 −24.933 −7.183 1.00 33.87 BBBB ATOM 4974 ND2 ASN B 317 29.170 −27.171 −6.933 1.00 35.63 BBBB ATOM 4975 C ASN B 317 27.270 −25.310 − 11.026 1.00 27.23 BBBB ATOM 4976 O ASN B 317 27.887 −24.543 − 11.765 1.00 26.36 BBBB ATOM 4977 N THR B 318 26.424 −26.224 − 11.482 1.00 26.95 BBBB ATOM 4978 CA THR B 318 26.174 −26.371 − 12.906 1.00 27.04 BBBB ATOM 4979 CB THR B 318 25.203 −27.537 − 13.189 1.00 27.91 BBBB ATOM 4980 OG1 THR B 318 25.843 −28.779 − 12.872 1.00 30.24 BBBB ATOM 4981 CG2 THR B 318 24.784 −27.539 − 14.655 1.00 27.49 BBBB ATOM 4982 C THR B 318 25.579 −25.087 − 13.480 1.00 26.50 BBBB ATOM 4983 O THR B 318 26.085 −24.548 − 14.465 1.00 26.71 BBBB ATOM 4984 N LEU B 319 24.516 −24.588 − 12.859 1.00 24.75 BBBB ATOM 4985 CA LEU B 319 23.883 −23.370 − 13.357 1.00 25.21 BBBB ATOM 4986 CB LEU B 319 22.579 −23.090 − 12.600 1.00 23.70 BBBB ATOM 4987 CG LEU B 319 21.496 −24.153 − 12.803 1.00 23.20 BBBB ATOM 4988 CD1 LEU B 319 20.384 −23.962 − 11.785 1.00 22.93 BBBB ATOM 4989 CD2 LEU B 319 20.963 −24.065 − 14.237 1.00 22.39 BBBB ATOM 4990 C LEU B 319 24.814 −22.169 − 13.253 1.00 25.23 BBBB ATOM 4991 O LEU B 319 24.888 −21.368 − 14.168 1.00 25.17 BBBB ATOM 4992 N ALA B 320 25.540 −22.055 − 12.147 1.00 24.41 BBBB ATOM 4993 CA ALA B 320 26.445 − 20.931 − 11.957 1.00 24.59 BBBB ATOM 4994 CB ALA B 320 27.069 − 20.987 − 10.547 1.00 24.46 BBBB ATOM 4995 C ALA B 320 27.549 − 20.865 − 13.010 1.00 24.21 BBBB ATOM 4996 O ALA B 320 28.091 − 19.800 − 13.281 1.00 24.35 BBBB ATOM 4997 N GLY B 321 27.878 −22.005 − 13.601 1.00 24.35 BBBB ATOM 4998 CA GLY B 321 28.934 −22.031 − 14.591 1.00 24.34 BBBB ATOM 4999 C GLY B 321 28.509 −21.642 − 15.993 1.00 24.34 BBBB ATOM 5000 O GLY B 321 29.345 −21.585 − 16.890 1.00 24.63 BBBB ATOM 5001 N TRP B 322 27.225 −21.357 − 16.188 1.00 22.62 BBBB ATOM 5002 CA TRP B 322 26.738 −21.007 − 17.521 1.00 21.72 BBBB ATOM 5003 CB TRP B 322 25.499 −21.841 − 17.858 1.00 20.09 BBBB ATOM 5004 CG TRP B 322 25.763 −23.318 − 17.973 1.00 19.85 BBBB ATOM 5005 CD2 TRP B 322 24.789 −24.370 − 17.939 1.00 19.16 BBBB ATOM 5006 CE2 TRP B 322 25.479 −25.584 − 18.164 1.00 20.31 BBBB ATOM 5007 CE3 TRP B 322 23.403 −24.406 − 17.742 1.00 19.35 BBBB ATOM 5008 CD1 TRP B 322 26.973 −23.925 − 18.204 1.00 19.51 BBBB ATOM 5009 NE1 TRP B 322 26.806 −25.281 − 18.323 1.00 18.84 BBBB ATOM 5010 CZ2 TRP B 322 24.825 −26.825 − 18.198 1.00 20.00 BBBB ATOM 5011 CZ3 TRP B 322 22.749 −25.646 − 17.775 1.00 19.90 BBBB ATOM 5012 CH2 TRP B 322 23.467 −26.836 − 18.003 1.00 20.26 BBBB ATOM 5013 C TRP B 322 26.422 − 19.524 − 17.722 1.00 21.61 BBBB ATOM 5014 O TRP B 322 25.390 − 19.030 − 17.271 1.00 21.25 BBBB ATOM 5015 N SER B 323 27.320 − 18.824 − 18.409 1.00 19.53 BBBB ATOM 5016 CA SER B 323 27.141 − 17.404 − 18.692 1.00 19.04 BBBB ATOM 5017 CB SER B 323 28.456 − 16.807 − 19.186 1.00 18.51 BBBB ATOM 5018 OG SER B 323 28.793 − 17.374 − 20.447 1.00 16.33 BBBB ATOM 5019 C SER B 323 26.099 − 17.239 − 19.799 1.00 18.26 BBBB ATOM 5020 O SER B 323 25.690 − 18.216 − 20.426 1.00 16.71 BBBB ATOM 5021 N ARG B 324 25.690 − 15.999 − 20.053 1.00 19.12 BBBB ATOM 5022 CA ARG B 324 24.725 − 15.741 −21.112 1.00 18.09 BBBB ATOM 5023 CB ARG B 324 24.298 − 14.268 −21.108 1.00 19.15 BBBB ATOM 5024 CG ARG B 324 23.266 − 13.973 − 20.031 1.00 20.58 BBBB ATOM 5025 CD ARG B 324 22.508 − 12.662 − 20.220 1.00 22.13 BBBB ATOM 5026 NE ARG B 324 21.345 − 12.641 − 19.331 1.00 21.36 BBBB ATOM 5027 CZ ARG B 324 20.268 − 13.403 − 19.510 1.00 21.63 BBBB ATOM 5028 NH1 ARG B 324 20.206 − 14.224 − 20.549 1.00 20.63 BBBB ATOM 5029 NH2 ARG B 324 19.269 − 13.378 − 18.633 1.00 22.19 BBBB ATOM 5030 C ARG B 324 25.288 − 16.145 −22.481 1.00 17.79 BBBB ATOM 5031 O ARG B 324 24.540 − 16.611 −23.341 1.00 17.56 BBBB ATOM 5032 N GLU B 325 26.597 − 15.975 −22.686 1.00 17.74 BBBB ATOM 5033 CA GLU B 325 27.220 − 16.368 −23.954 1.00 16.96 BBBB ATOM 5034 CB GLU B 325 28.690 − 15.907 −24.028 1.00 17.92 BBBB ATOM 5035 CG GLU B 325 29.361 − 16.398 −25.319 1.00 18.50 BBBB ATOM 5036 CD GLU B 325 30.844 − 16.068 −25.454 1.00 19.03 BBBB ATOM 5037 OE1 GLU B 325 31.446 − 16.562 −26.433 1.00 18.89 BBBB ATOM 5038 OE2 GLU B 325 31.408 − 15.325 −24.615 1.00 20.56 BBBB ATOM 5039 C GLU B 325 27.164 − 17.894 −24.110 1.00 16.65 BBBB ATOM 5040 O GLU B 325 26.838 − 18.428 −25.172 1.00 15.39 BBBB ATOM 5041 N THR B 326 27.500 − 18.603 −23.042 1.00 16.67 BBBB ATOM 5042 CA THR B 326 27.460 − 20.055 −23.070 1.00 16.39 BBBB ATOM 5043 CB THR B 326 27.967 − 20.635 −21.725 1.00 16.62 BBBB ATOM 5044 OG1 THR B 326 29.346 − 20.294 −21.561 1.00 18.31 BBBB ATOM 5045 CG2 THR B 326 27.804 −22.143 −21.690 1.00 18.20 BBBB ATOM 5046 C THR B 326 26.034 − 20.551 −23.321 1.00 17.40 BBBB ATOM 5047 O THR B 326 25.817 −21.478 −24.107 1.00 16.65 BBBB ATOM 5048 N LEU B 327 25.068 − 19.932 −22.643 1.00 17.90 BBBB ATOM 5049 CA LEU B 327 23.659 − 20.305 −22.780 1.00 17.27 BBBB ATOM 5050 CB LEU B 327 22.791 − 19.514 −21.791 1.00 17.35 BBBB ATOM 5051 CG LEU B 327 22.922 − 19.919 − 20.309 1.00 16.74 BBBB ATOM 5052 CD1 LEU B 327 22.192 − 18.930 − 19.416 1.00 14.82 BBBB ATOM 5053 CD2 LEU B 327 22.361 −21.312 − 20.129 1.00 18.13 BBBB ATOM 5054 C LEU B 327 23.145 − 20.096 −24.198 1.00 17.58 BBBB ATOM 5055 O LEU B 327 22.352 − 20.899 −24.692 1.00 16.08 BBBB ATOM 5056 N LEU B 328 23.584 − 19.014 −24.845 1.00 17.87 BBBB ATOM 5057 CA LEU B 328 23.175 − 18.745 −26.222 1.00 17.39 BBBB ATOM 5058 CB LEU B 328 23.706 − 17.379 −26.690 1.00 17.84 BBBB ATOM 5059 CG LEU B 328 23.475 − 17.021 −28.173 1.00 18.65 BBBB ATOM 5060 CD1 LEU B 328 21.988 − 17.112 −28.494 1.00 16.92 BBBB ATOM 5061 CD2 LEU B 328 23.984 − 15.608 −28.460 1.00 18.47 BBBB ATOM 5062 C LEU B 328 23.716 − 19.868 −27.111 1.00 17.74 BBBB ATOM 5063 O LEU B 328 23.003 − 20.400 −27.953 1.00 17.59 BBBB ATOM 5064 N THR B 329 24.977 − 20.244 −26.910 1.00 20.12 BBBB ATOM 5065 CA THR B 329 25.567 −21.335 −27.688 1.00 21.30 BBBB ATOM 5066 CB THR B 329 27.069 −21.556 −27.336 1.00 22.69 BBBB ATOM 5067 OG1 THR B 329 27.866 − 20.591 −28.029 1.00 25.80 BBBB ATOM 5068 CG2 THR B 329 27.533 −22.957 −27.757 1.00 24.48 BBBB ATOM 5069 C THR B 329 24.819 −22.644 −27.457 1.00 20.40 BBBB ATOM 5070 O THR B 329 24.552 −23.382 −28.398 1.00 20.34 BBBB ATOM 5071 N MET B 330 24.494 −22.933 −26.200 1.00 20.31 BBBB ATOM 5072 CA MET B 330 23.771 −24.153 −25.870 1.00 19.91 BBBB ATOM 5073 CB MET B 330 23.642 −24.292 −24.350 1.00 20.88 BBBB ATOM 5074 CG MET B 330 24.957 −24.571 −23.647 1.00 21.37 BBBB ATOM 5075 SD MET B 330 24.805 −24.609 −21.855 1.00 22.76 BBBB ATOM 5076 CE MET B 330 24.118 −26.250 −21.622 1.00 22.37 BBBB ATOM 5077 C MET B 330 22.389 −24.149 −26.519 1.00 19.43 BBBB ATOM 5078 O MET B 330 21.924 −25.167 −27.029 1.00 20.85 BBBB ATOM 5079 N ALA B 331 21.737 −22.996 −26.504 1.00 18.81 BBBB ATOM 5080 CA ALA B 331 20.412 −22.871 −27.098 1.00 18.49 BBBB ATOM 5081 CB ALA B 331 19.868 −21.462 −26.859 1.00 17.16 BBBB ATOM 5082 C ALA B 331 20.481 −23.162 −28.594 1.00 19.04 BBBB ATOM 5083 O ALA B 331 19.644 −23.879 −29.130 1.00 18.16 BBBB ATOM 5084 N GLU B 332 21.489 −22.613 −29.269 1.00 19.87 BBBB ATOM 5085 CA GLU B 332 21.626 −22.827 −30.704 1.00 21.47 BBBB ATOM 5086 CB GLU B 332 22.709 −21.912 −31.274 1.00 22.13 BBBB ATOM 5087 CG GLU B 332 22.328 − 20.455 −31.143 1.00 24.10 BBBB ATOM 5088 CD GLU B 332 23.428 − 19.522 −31.572 1.00 26.61 BBBB ATOM 5089 OE1 GLU B 332 24.594 − 19.765 −31.197 1.00 26.92 BBBB ATOM 5090 OE2 GLU B 332 23.118 − 18.542 −32.273 1.00 27.58 BBBB ATOM 5091 C GLU B 332 21.921 −24.280 −31.025 1.00 22.44 BBBB ATOM 5092 O GLU B 332 21.412 −24.814 −32.006 1.00 22.84 BBBB ATOM 5093 N ARG B 333 22.739 −24.923 −30.200 1.00 22.30 BBBB ATOM 5094 CA ARG B 333 23.040 −26.330 −30.408 1.00 23.77 BBBB ATOM 5095 CB ARG B 333 24.117 −26.789 −29.427 1.00 25.03 BBBB ATOM 5096 CG ARG B 333 25.503 −26.222 −29.737 1.00 26.79 BBBB ATOM 5097 CD ARG B 333 26.443 −26.467 −28.570 1.00 28.88 BBBB ATOM 5098 NE ARG B 333 27.810 −26.041 −28.846 1.00 29.09 BBBB ATOM 5099 CZ ARG B 333 28.772 −26.001 −27.932 1.00 30.32 BBBB ATOM 5100 NH1 ARG B 333 28.514 −26.361 −26.678 1.00 32.07 BBBB ATOM 5101 NH2 ARG B 333 29.990 −25.596 −28.269 1.00 31.36 BBBB ATOM 5102 C ARG B 333 21.763 −27.147 −30.218 1.00 23.13 BBBB ATOM 5103 O ARG B 333 21.548 −28.151 −30.895 1.00 23.45 BBBB ATOM 5104 N ALA B 334 20.907 −26.713 −29.299 1.00 22.82 BBBB ATOM 5105 CA ALA B 334 19.648 −27.420 −29.063 1.00 22.88 BBBB ATOM 5106 CB ALA B 334 18.915 −26.800 −27.882 1.00 22.08 BBBB ATOM 5107 C ALA B 334 18.778 −27.333 −30.317 1.00 22.86 BBBB ATOM 5108 O ALA B 334 18.285 −28.339 −30.827 1.00 21.38 BBBB ATOM 5109 N ARG B 335 18.602 −26.114 −30.815 1.00 23.14 BBBB ATOM 5110 CA ARG B 335 17.795 −25.892 −32.002 1.00 23.54 BBBB ATOM 5111 CB ARG B 335 17.815 −24.407 −32.361 1.00 25.17 BBBB ATOM 5112 CG ARG B 335 16.804 −23.995 −33.418 1.00 26.90 BBBB ATOM 5113 CD ARG B 335 15.381 −24.129 −32.891 1.00 30.87 BBBB ATOM 5114 NE ARG B 335 14.435 −23.414 −33.736 1.00 33.71 BBBB ATOM 5115 CZ ARG B 335 13.607 −22.469 −33.301 1.00 35.57 BBBB ATOM 5116 NH1 ARG B 335 13.601 −22.123 −32.016 1.00 34.54 BBBB ATOM 5117 NH2 ARG B 335 12.791 −21.862 −34.157 1.00 35.17 BBBB ATOM 5118 C ARG B 335 18.348 −26.724 −33.163 1.00 23.86 BBBB ATOM 5119 O ARG B 335 17.595 −27.360 −33.902 1.00 22.38 BBBB ATOM 5120 N ALA B 336 19.671 −26.737 −33.297 1.00 25.17 BBBB ATOM 5121 CA ALA B 336 20.330 −27.477 −34.372 1.00 26.85 BBBB ATOM 5122 CB ALA B 336 21.830 −27.174 −34.374 1.00 26.27 BBBB ATOM 5123 C ALA B 336 20.101 −28.985 −34.288 1.00 27.80 BBBB ATOM 5124 O ALA B 336 20.052 −29.665 −35.308 1.00 27.33 BBBB ATOM 5125 N ALA B 337 19.959 −29.501 −33.072 1.00 29.45 BBBB ATOM 5126 CA ALA B 337 19.740 −30.925 −32.865 1.00 30.89 BBBB ATOM 5127 CB ALA B 337 20.205 −31.320 −31.467 1.00 31.47 BBBB ATOM 5128 C ALA B 337 18.267 −31.276 −33.047 1.00 32.47 BBBB ATOM 5129 O ALA B 337 17.887 −32.445 −33.029 1.00 34.14 BBBB ATOM 5130 N SER B 338 17.442 −30.254 −33.229 1.00 31.76 BBBB ATOM 5131 CA SER B 338 16.008 −30.432 −33.408 1.00 32.41 BBBB ATOM 5132 CB SER B 338 15.286 −29.140 −33.029 1.00 31.94 BBBB ATOM 5133 OG SER B 338 13.921 −29.196 −33.385 1.00 34.53 BBBB ATOM 5134 C SER B 338 15.593 −30.822 −34.829 1.00 33.16 BBBB ATOM 5135 C SER B 338 16.274 −30.503 −35.801 1.00 32.25 BBBB ATOM 5136 N ILE B 339 14.466 −31.523 −34.921 1.00 33.44 BBBB ATOM 5137 CA ILE B 339 13.882 −31.941 −36.187 1.00 34.35 BBBB ATOM 5138 CB ILE B 339 13.989 −33.472 −36.384 1.00 35.51 BBBB ATOM 5139 CG2 lLE B 339 13.271 −33.880 −37.658 1.00 35.53 BBBB ATOM 5140 CG1 ILE B 339 15.463 −33.887 −36.450 1.00 36.09 BBBB ATOM 5141 CD1 ILE B 339 15.688 −35.378 −36.667 1.00 37.71 BBBB ATOM 5142 C ILE B 339 12.416 −31.518 −36.059 1.00 34.84 BBBB ATOM 5143 O ILE B 339 11.601 −32.229 −35.479 1.00 35.09 BBBB ATOM 5144 N PRO B 340 12.068 −30.344 −36.611 1.00 34.93 BBBB ATOM 5145 CD PRO B 340 12.999 −29.525 −37.409 1.00 35.06 BBBB ATOM 5146 CA PRO B 340 10.733 −29.730 −36.600 1.00 34.94 BBBB ATOM 5147 CB PRO B 340 10.994 −28.349 −37.194 1.00 35.58 BBBB ATOM 5148 CG PRO B 340 12.052 −28.642 −38.205 1.00 36.27 BBBB ATOM 5149 C PRO B 340 9.551 −30.409 −37.284 1.00 34.07 BBBB ATOM 5150 O PRO B 340 8.410 −30.222 −36.861 1.00 34.18 BBBB ATOM 5151 N ASP B 341 9.803 −31.180 −38.334 1.00 33.42 BBBB ATOM 5152 CA ASP B 341 8.711 −31.820 −39.056 1.00 33.33 BBBB ATOM 5153 CB ASP B 341 8.802 −31.448 −40.536 1.00 35.03 BBBB ATOM 5154 CG ASP B 341 10.101 −31.886 −41.159 1.00 37.02 BBBB ATOM 5155 OD1 ASP B 341 11.125 −31.907 −40.443 1.00 37.17 BBBB ATOM 5156 OD2 ASP B 341 10.102 −32.200 −42.367 1.00 40.57 BBBB ATOM 5157 C ASP B 341 8.655 −33.336 −38.899 1.00 32.11 BBBB ATOM 5158 O ASP B 341 8.377 −34.066 −39.854 1.00 30.74 BBBB ATOM 5159 N ALA B 342 8.908 −33.807 −37.683 1.00 30.63 BBBB ATOM 5160 CA ALA B 342 8.875 −35.238 −37.411 1.00 29.09 BBBB ATOM 5161 CB ALA B 342 9.174 −35.496 −35.927 1.00 28.28 BBBB ATOM 5162 C ALA B 342 7.530 −35.844 −37.792 1.00 28.32 BBBB ATOM 5163 O ALA B 342 7.475 −36.901 −38.416 1.00 29.88 BBBB ATOM 5164 N THR B 343 6.441 −35.177 −37.427 1.00 28.28 BBBB ATOM 5165 CA THR B 343 5.115 −35.696 −37.744 1.00 28.55 BBBB ATOM 5166 CB THR B 343 3.998 −34.765 −37.205 1.00 29.04 BBBB ATOM 5167 OG1 THR B 343 4.119 −34.642 −35.782 1.00 28.04 BBBB ATOM 5168 CG2 THR B 343 2.628 −35.330 −37.528 1.00 28.54 BBBB ATOM 5169 C THR B 343 4.934 −35.882 −39.254 1.00 29.50 BBBB ATOM 5170 O THR B 343 4.533 −36.952 −39.711 1.00 28.08 BBBB ATOM 5171 N GLU B 344 5.234 −34.843 −40.030 1.00 30.76 BBBB ATOM 5172 CA GLU B 344 5.085 −34.933 −41.480 1.00 32.00 BBBB ATOM 5173 CB GLU B 344 5.414 −33.589 −42.142 1.00 34.02 BBBB ATOM 5174 CG GLU B 344 4.412 −32.483 −41.814 1.00 38.27 BBBB ATOM 5175 CD GLU B 344 4.807 −31.661 −40.594 1.00 40.96 BBBB ATOM 5176 OE1 GLU B 344 5.252 −32.252 −39.582 1.00 41.33 BBBB ATOM 5177 OE2 GLU B 344 4.665 −30.419 −40.649 1.00 42.30 BBBB ATOM 5178 C GLU B 344 5.970 −36.032 −42.056 1.00 31.14 BBBB ATOM 5179 O GLU B 344 5.534 −36.805 −42.909 1.00 32.33 BBBB ATOM 5180 N ARG B 345 7.209 −36.106 −41.587 1.00 30.66 BBBB ATOM 5181 CA ARG B 345 8.138 −37.123 −42.067 1.00 31.44 BBBB ATOM 5182 CB ARG B 345 9.494 −36.986 −41.376 1.00 33.54 BBBB ATOM 5183 CG ARG B 345 10.293 −35.772 −41.793 1.00 37.73 BBBB ATOM 5184 CD ARG B 345 11.716 −35.880 −41.284 1.00 40.70 BBBB ATOM 5185 NE ARG B 345 12.580 −34.864 −41.873 1.00 44.36 BBBB ATOM 5186 CZ ARG B 345 13.901 −34.841 −41.739 1.00 45.65 BBBB ATOM 5187 NH1 ARG B 345 14.514 −35.782 −41.031 1.00 46.05 BBBB ATOM 5188 NH2 ARG B 345 14.608 −33.881 −42.322 1.00 47.38 BBBB ATOM 5189 C ARG B 345 7.626 −38.545 −41.854 1.00 30.89 BBBB ATOM 5190 O ARG B 345 7.724 −39.387 −42.746 1.00 29.98 BBBB ATOM 5191 N VAL B 346 7.086 −38.818 −40.670 1.00 29.72 BBBB ATOM 5192 CA VAL B 346 6.578 −40.151 −40.384 1.00 28.61 BBBB ATOM 5193 CB VAL B 346 6.197 −40.298 −38.885 1.00 27.90 BBBB ATOM 5194 CG1 VAL B 346 5.612 −41.680 −38.625 1.00 27.30 BBBB ATOM 5195 CG2 VAL B 346 7.419 −40.060 −38.024 1.00 27.32 BBBB ATOM 5196 C VAL B 346 5.361 −40.435 −41.252 1.00 28.33 BBBB ATOM 5197 O VAL B 346 5.248 −41.511 −41.847 1.00 28.30 BBBB ATOM 5198 N ALA B 347 4.457 −39.465 −41.335 1.00 28.76 BBBB ATOM 5199 CA ALA B 347 3.249 −39.617 −42.137 1.00 28.96 BBBB ATOM 5200 CB ALA B 347 2.363 −38.387 −41.994 1.00 28.49 BBBB ATOM 5201 C ALA B 347 3.596 −39.844 −43.606 1.00 30.26 BBBB ATOM 5202 O ALA B 347 2.948 −40.641 −44.279 1.00 30.12 BBBB ATOM 5203 N ASN B 348 4.613 −39.142 −44.098 1.00 32.77 BBBB ATOM 5204 CA ASN B 348 5.035 −39.286 −45.493 1.00 34.56 BBBB ATOM 5205 CB ASN B 348 6.045 −38.195 −45.868 1.00 35.68 BBBB ATOM 5206 CG ASN B 348 5.384 −36.846 −46.123 1.00 37.21 BBBB ATOM 5207 OD1 ASN B 348 4.157 −36.719 −46.081 1.00 38.48 BBBB ATOM 5208 ND2 ASN B 348 6.199 −35.831 −46.393 1.00 38.38 BBBB ATOM 5209 C ASN B 348 5.633 −40.668 −45.765 1.00 34.90 BBBB ATOM 5210 O ASN B 348 5.433 −41.233 −46.841 1.00 34.59 BBBB ATOM 5211 N GLU B 349 6.366 −41.212 −44.794 1.00 35.20 BBBB ATOM 5212 CA GLU B 349 6.954 −42.540 −44.956 1.00 34.86 BBBB ATOM 5213 CB GLU B 349 8.004 −42.814 −43.879 1.00 34.59 BBBB ATOM 5214 CG GLU B 349 9.404 −42.385 −44.259 1.00 38.16 BBBB ATOM 5215 CD GLU B 349 9.865 −42.992 −45.579 1.00 38.74 BBBB ATOM 5216 OE1 GLU B 349 9.806 −44.232 −45.735 1.00 40.12 BBBB ATOM 5217 OE2 GLU B 349 10.292 −42.225 −46.461 1.00 39.64 BBBB ATOM 5218 C GLU B 349 5.872 −43.607 −44.895 1.00 33.96 BBBB ATOM 5219 O GLU B 349 5.942 −44.621 −45.591 1.00 33.99 BBBB ATOM 5220 N VAL B 350 4.875 −43.377 −44.051 1.00 33.91 BBBB ATOM 5221 CA VAL B 350 3.767 −44.306 −43.919 1.00 33.79 BBBB ATOM 5222 CB VAL B 350 2.848 −43.907 −42.744 1.00 33.70 BBBB ATOM 5223 CG1 VAL B 350 1.554 −44.695 −42.798 1.00 32.22 BBBB ATOM 5224 CG2 VAL B 350 3.568 −44.154 −41.425 1.00 32.24 BBBB ATOM 5225 C VAL B 350 2.969 −44.274 −45.217 1.00 34.78 BBBB ATOM 5226 O VAL B 350 2.411 −45.285 −45.645 1.00 34.85 BBBB ATOM 5227 N SER B 351 2.925 −43.102 −45.844 1.00 35.34 BBBB ATOM 5228 CA SER B 351 2.196 −42.946 −47.095 1.00 36.67 BBBB ATOM 5229 CB SER B 351 2.024 −41.462 −47.425 1.00 37.32 BBBB ATOM 5230 OG SER B 351 1.241 −41.292 −48.590 1.00 37.74 BBBB ATOM 5231 C SER B 351 2.958 −43.639 −48.222 1.00 37.35 BBBB ATOM 5232 O SER B 351 2.365 −44.309 −49.064 1.00 36.85 BBBB ATOM 5233 N ARG B 352 4.277 −43.482 −48.223 1.00 37.89 BBBB ATOM 5234 CA ARG B 352 5.114 −44.088 −49.251 1.00 40.03 BBBB ATOM 5235 CB ARG B 352 6.557 −43.600 −49.114 1.00 41.58 BBBB ATOM 5236 CG ARG B 352 7.470 −44.069 −50.232 1.00 44.46 BBBB ATOM 5237 CD ARG B 352 8.906 −44.157 −49.759 1.00 47.36 BBBB ATOM 5238 NE ARG B 352 9.097 −45.271 −48.832 1.00 49.57 BBBB ATOM 5239 CZ ARG B 352 10.234 −45.524 −48.191 1.00 50.54 BBBB ATOM 5240 NH1 ARG B 352 11.287 −44.738 −48.372 1.00 50.88 BBBB ATOM 5241 NH2 ARG B 352 10.321 −46.566 −47.373 1.00 50.24 BBBB ATOM 5242 C ARG B 352 5.098 −45.613 −49.176 1.00 40.60 BBBB ATOM 5243 O ARG B 352 5.101 −46.292 −50.204 1.00 39.84 BBBB ATOM 5244 N VAL B 353 5.096 −46.143 −47.955 1.00 41.33 BBBB ATOM 5245 CA VAL B 353 5.089 −47.587 −47.737 1.00 42.78 BBBB ATOM 5246 CB VAL B 353 5.446 −47.927 −46.271 1.00 42.54 BBBB ATOM 5247 CG1 VAL B 353 5.279 −49.420 −46.014 1.00 42.05 BBBB ATOM 5248 CG2 VAL B 353 6.879 −47.509 −45.987 1.00 41.86 BBBB ATOM 5249 C VAL B 353 3.742 −48.206 −48.095 1.00 43.85 BBBB ATOM 5250 O VAL B 353 3.679 −49.343 −48.556 1.00 44.43 BBBB ATOM 5251 N ALA B 354 2.664 −47.465 −47.871 1.00 45.85 BBBB ATOM 5252 CA ALA B 354 1.336 −47.957 −48.212 1.00 47.24 BBBB ATOM 5253 CB ALA B 354 0.264 −47.043 −47.628 1.00 46.79 BBBB ATOM 5254 C ALA B 354 1.250 −47.971 −49.737 1.00 48.54 BBBB ATOM 5255 O ALA B 354 0.531 −48.780 −50.324 1.00 48.48 BBBB ATOM 5256 N ARG B 355 1.998 −47.068 −50.366 1.00 50.49 BBBB ATOM 5257 CA ARG B 355 2.035 −46.964 −51.824 1.00 52.71 BBBB ATOM 5258 CB ARG B 355 2.658 −45.633 −52.264 1.00 53.58 BBBB ATOM 5259 CG ARG B 355 1.998 −44.372 −51.730 1.00 55.08 BBBB ATOM 5260 CD ARG B 355 0.716 −44.014 −52.461 1.00 56.64 BBBB ATOM 5261 NE ARG B 355 0.112 −42.802 −51.907 1.00 57.43 BBBB ATOM 5262 CZ ARG B 355 −1.054 −42.296 −52.299 1.00 58.24 BBBB ATOM 5263 NH1 ARG B 355 −1.758 −42.896 −53.252 1.00 58.53 BBBB ATOM 5264 NH2 ARG B 355 −1.519 −41.186 −51.738 1.00 58.87 BBBB ATOM 5265 C ARG B 355 2.899 −48.099 −52.366 1.00 53.41 BBBB ATOM 5266 O ARG B 355 2.966 −48.319 −53.575 1.00 53.50 BBBB ATOM 5267 N ALA B 356 3.569 −48.805 −51.456 1.00 54.15 BBBB ATOM 5268 CA ALA B 356 4.453 −49.913 −51.809 1.00 54.93 BBBB ATOM 5269 CB ALA B 356 3.669 −51.004 −52.546 1.00 54.86 BBBB ATOM 5270 C ALA B 356 5.611 −49.417 −52.671 1.00 55.63 BBBB ATOM 5271 O ALA B 356 6.193 −50.178 −53.442 1.00 55.95 BBBB ATOM 5272 N LEU B 357 5.942 −48.136 −52.526 1.00 56.45 BBBB ATOM 5273 CA LEU B 357 7.023 −47.522 −53.289 1.00 57.81 BBBB ATOM 5274 CB LEU B 357 6.871 −45.997 −53.290 1.00 58.04 BBBB ATOM 5275 CG LEU B 357 5.595 −45.422 −53.915 1.00 58.29 BBBB ATOM 5276 CD1 LEU B 357 5.624 −43.903 −53.820 1.00 58.36 BBBB ATOM 5277 CD2 LEU B 357 5.485 −45.859 −55.370 1.00 58.62 BBBB ATOM 5278 C LEU B 357 8.391 −47.895 −52.729 1.00 58.46 BBBB ATOM 5279 OT1 LEU B 357 9.244 −48.359 −53.514 1.00 58.97 BBBB ATOM 5280 OT2 LEU B 357 8.601 −47.710 −51.512 1.00 58.97 BBBB ATOM 5281 OH2 WAT W 1 −20.568 11.549 41.653 1.00 24.11 WATR ATOM 5282 OH2 WAT W 4 −7.219 −67.275 −41.843 1.00 35.35 WATR ATOM 5283 OH2 WAT W 5 20.119 −17.520 −22.473 1.00 21.13 WATR ATOM 5284 OH2 WAT W 6 18.858 −19.701 −23.468 1.00 18.31 WATR ATOM 5285 OH2 WAT W 7 2.329 −28.724 − 15.978 1.00 27.32 WATR ATOM 5286 OH2 WAT W 8 9.484 −48.435 −27.938 1.00 23.67 WATR ATOM 5287 OH2 WAT W 9 7.645 −57.693 −27.177 1.00 21.03 WATR ATOM 5288 OH2 WAT W 10 −1.542 −8.422 1.824 1.00 29.71 WATR ATOM 5289 OH2 WAT W 11 5.875 −50.793 −32.396 1.00 20.21 WATR ATOM 5290 OH2 WAT W 12 27.592 − 18.174 −27.779 1.00 22.52 WATR ATOM 5291 OH2 WAT W 13 7.842 −13.432 −21.178 1.00 25.85 WATR ATOM 5292 OH2 WAT W 14 4.845 −57.924 −27.444 1.00 24.35 WATR ATOM 5293 OH2 WAT W 15 0.473 −58.751 − 17.746 1.00 35.49 WATR ATOM 5294 OH2 WAT W 16 7.998 −52.522 −25.785 1.00 22.34 WATR ATOM 5295 OH2 WAT W 17 −8.656 11.300 18.872 1.00 23.81 WATR ATOM 5296 OH2 WAT W 18 8.711 −45.913 −29.121 1.00 21.55 WATR ATOM 5297 OH2 WAT W 19 2.957 −68.158 −38.242 1.00 29.43 WATR ATOM 5298 OH2 WAT W 20 16.486 −11.742 −16.567 1.00 22.13 WATR ATOM 5299 OH2 WAT W 21 −6.251 17.702 28.534 1.00 24.24 WATR ATOM 5300 OH2 WAT W 22 12.670 −47.636 −24.808 1.00 25.87 WATR ATOM 5301 OH2 WAT W 23 6.513 −15.597 −22.517 1.00 26.31 WATR ATOM 5302 OH2 WAT W 24 7.536 −66.906 −21.753 1.00 21.48 WATR ATOM 5303 OH2 WAT W 25 −29.060 13.621 26.406 1.00 21.08 WATR ATOM 5304 OH2 WAT W 26 −5.240 10.154 13.527 1.00 29.62 WATR ATOM 5305 OH2 WAT W 27 29.942 −20.139 −19.237 1.00 20.38 WATR ATOM 5306 OH2 WAT W 28 18.996 −28.763 −24.427 1.00 20.28 WATR ATOM 5307 OH2 WAT W 29 8.755 −51.080 −27.990 1.00 20.66 WATR ATOM 5308 OH2 WAT W 30 4.215 −64.684 −43.328 1.00 39.67 WATR ATOM 5309 OH2 WAT W 31 14.708 − 11.936 −1.749 1.00 24.57 WATR ATOM 5310 OH2 WAT W 32 28.140 −13.870 −21.266 1.00 18.93 WATR ATOM 5311 OH2 WAT W 33 4.057 −1.221 9.809 1.00 32.30 WATR ATOM 5312 OH2 WAT W 34 4.784 −56.759 −43.904 1.00 25.99 WATR ATOM 5313 OH2 WAT W 35 −22.733 10.283 33.238 1.00 24.60 WATR ATOM 5314 OH2 WAT W 36 0.540 14.225 10.932 1.00 26.89 WATR ATOM 5315 OH2 WAT W 37 −7.560 11.931 12.593 1.00 27.76 WATR ATOM 5316 OH2 WAT W 38 −7.966 17.043 30.555 1.00 20.04 WATR ATOM 5317 OH2 WAT W 39 6.716 −55.314 −42.959 1.00 25.72 WATR ATOM 5318 OH2 WAT W 40 6.833 −32.402 −3.845 1.00 32.49 WATR ATOM 5319 OH2 WAT W 41 30.445 − 20.104 −25.459 1.00 27.97 WATR ATOM 5320 OH2 WAT W 42 1.475 −15.304 −22.128 1.00 30.57 WATR ATOM 5321 OH2 WAT W 43 15.703 −42.835 −31.237 1.00 26.74 WATR ATOM 5322 OH2 WAT W 44 7.131 −6.595 − 18.003 1.00 29.47 WATR ATOM 5323 OH2 WAT W 45 30.256 −23.202 −11.163 1.00 33.81 WATR ATOM 5324 OH2 WAT W 46 −6.107 −66.004 −38.690 1.00 30.45 WATR ATOM 5325 OH2 WAT W 47 17.631 −17.241 −5.864 1.00 28.69 WATR ATOM 5326 OH2 WAT W 48 13.436 −59.821 −27.855 1.00 28.71 WATR ATOM 5327 OH2 WAT W 49 11.395 −15.293 2.925 1.00 29.36 WATR ATOM 5328 OH2 WAT W 50 19.218 −21.377 −34.248 1.00 31.41 WATR ATOM 5329 OH2 WAT W 51 11.973 − 11.890 −15.788 1.00 35.59 WATR ATOM 5330 OH2 WAT W 52 9.140 −8.260 −23.371 1.00 40.29 WATR ATOM 5331 OH2 WAT W 53 −19.061 14.438 38.966 1.00 38.01 WATR ATOM 5332 OH2 WAT W 54 −3.895 −70.510 −28.249 1.00 25.56 WATR ATOM 5333 OH2 WAT W 55 20.909 −23.456 −34.213 1.00 26.74 WATR ATOM 5334 OH2 WAT W 56 −8.505 11.136 10.323 1.00 30.97 WATR ATOM 5335 OH2 WAT W 57 22.022 −15.529 −23.223 1.00 26.74 WATR ATOM 5336 OH2 WAT W 58 13.860 −49.304 −42.490 1.00 27.91 WATR ATOM 5337 OH2 WAT W 59 −9.455 −6.552 −9.720 1.00 41.70 WATR ATOM 5338 OH2 WAT W 60 13.798 −49.732 −23.016 1.00 41.60 WATR ATOM 5339 OH2 WAT W 61 15.881 −60.461 −31.910 1.00 48.66 WATR ATOM 5340 OH2 WAT W 62 −9.797 12.718 13.997 1.00 29.14 WATR ATOM 5341 OH2 WAT W 63 16.793 0.356 −6.115 1.00 26.17 WATR ATOM 5342 OH2 WAT W 64 3.173 18.778 20.793 1.00 31.13 WATR ATOM 5343 OH2 WAT W 65 13.433 −11.079 0.672 1.00 27.40 WATR ATOM 5344 OH2 WAT W 66 3.118 −0.813 0.729 1.00 24.68 WATR ATOM 5345 OH2 WAT W 67 −22.179 3.583 26.978 1.00 32.28 WATR ATOM 5346 OH2 WAT W 68 24.433 −30.481 −1.783 1.00 41.91 WATR ATOM 5347 OH2 WAT W 69 4.384 −66.131 −41.203 1.00 34.75 WATR ATOM 5348 OH2 WAT W 70 20.398 −7.386 −4.280 1.00 30.85 WATR ATOM 5349 OH2 WAT W 71 −2.444 −70.752 −22.067 1.00 25.46 WATR ATOM 5350 OH2 WAT W 72 −3.963 −4.914 −5.711 1.00 29.67 WATR ATOM 5351 OH2 WAT W 73 17.663 −11.040 −34.488 1.00 30.24 WATR ATOM 5352 OH2 WAT W 74 21.404 −42.041 −26.621 1.00 31.41 WATR ATOM 5353 OH2 WAT W 75 −1.110 −15.319 −1.089 1.00 31.51 WATR ATOM 5354 OH2 WAT W 76 0.688 19.730 22.519 1.00 26.71 WATR ATOM 5355 OH2 WAT W 77 12.113 −69.335 −26.593 1.00 27.11 WATR ATOM 5356 OH2 WAT W 78 11.725 −25.065 −33.817 1.00 43.79 WATR ATOM 5357 OH2 WAT W 79 −25.519 9.450 22.092 1.00 28.18 WATR ATOM 5358 OH2 WAT W 80 −14.673 6.584 16.023 1.00 31.37 WATR ATOM 5359 OH2 WAT W 81 −2.250 −0.253 −1.741 1.00 29.99 WATR ATOM 5360 OH2 WAT W 82 −7.300 12.943 8.415 1.00 32.39 WATR ATOM 5361 OH2 WAT W 83 1.712 −13.629 −13.904 1.00 34.08 WATR ATOM 5362 OH2 WAT W 84 4.709 −17.478 −6.557 1.00 29.67 WATR ATOM 5363 OH2 WAT W 85 10.070 −57.496 −44.450 1.00 48.39 WATR ATOM 5364 OH2 WAT W 86 8.040 −30.281 −10.117 1.00 28.59 WATR ATOM 5365 OH2 WAT W 87 −1.967 −32.372 −38.643 1.00 31.55 WATR ATOM 5366 OH2 WAT W 88 −3.178 −64.576 −25.506 1.00 33.66 WATR ATOM 5367 OH2 WAT W 89 15.762 −9.860 −10.400 1.00 34.29 WATR ATOM 5368 OH2 WAT W 90 5.654 −30.990 −27.758 1.00 35.84 WATR ATOM 5369 OH2 WAT W 91 14.959 −46.096 −42.270 1.00 35.21 WATR ATOM 5370 OH2 WAT W 92 10.137 −13.308 −9.753 1.00 32.65 WATR ATOM 5371 OH2 WAT W 93 −4.480 6.624 6.614 1.00 27.37 WATR ATOM 5372 OH2 WAT W 94 −14.574 22.522 18.870 1.00 49.48 WATR ATOM 5373 OH2 WAT W 95 −11.031 −42.768 −39.637 1.00 37.63 WATR ATOM 5374 OH2 WAT W 96 9.906 −35.479 − 19.203 1.00 29.59 WATR ATOM 5375 OH2 WAT W 97 −0.990 −0.781 36.951 1.00 37.27 WATR ATOM 5376 OH2 WAT W 98 −11.422 9.059 11.252 1.00 30.43 WATR ATOM 5377 OH2 WAT W 99 8.118 −36.710 −22.371 1.00 34.85 WATR ATOM 5378 OH2 WAT W 100 12.414 −67.326 −22.791 1.00 31.24 WATR ATOM 5379 OH2 WAT W 101 28.541 −24.603 −31.049 1.00 40.14 WATR ATOM 5380 OH2 WAT W 102 16.276 −10.934 −3.673 1.00 33.80 WATR ATOM 5381 OH2 WAT W 103 30.979 − 13.264 −22.953 1.00 24.73 WATR ATOM 5382 OH2 WAT W 104 12.759 −31.636 −31.838 1.00 26.40 WATR ATOM 5383 OH2 WAT W 105 23.507 −29.661 −32.187 1.00 29.62 WATR ATOM 5384 OH2 WAT W 106 21.292 − 13.141 −24.874 1.00 37.83 WATR ATOM 5385 OH2 WAT W 107 10.171 −32.960 −15.580 1.00 26.59 WATR ATOM 5386 OH2 WAT W 108 −2.207 2.376 2.034 1.00 27.55 WATR ATOM 5387 OH2 WAT W 109 −6.984 22.588 16.082 1.00 39.01 WATR ATOM 5388 OH2 WAT W 110 14.308 −11.038 −15.406 1.00 26.48 WATR ATOM 5389 OH2 WAT W 111 10.612 9.749 24.161 1.00 40.18 WATR ATOM 5390 OH2 WAT W 112 2.406 − 15.823 − 10.196 1.00 27.61 WATR ATOM 5391 OH2 WAT W 113 6.310 −68.984 − 20.661 1.00 40.25 WATR ATOM 5392 OH2 WAT W 114 14.379 −10.930 −8.565 1.00 35.86 WATR ATOM 5393 OH2 WAT W 115 24.183 −35.475 −30.338 1.00 35.17 WATR ATOM 5394 OH2 WAT W 116 21.897 −31.717 −1.243 1.00 47.61 WATR ATOM 5395 OH2 WAT W 117 24.065 − 17.545 −13.707 1.00 32.24 WATR ATOM 5396 OH2 WAT W 118 16.772 −51.926 −25.940 1.00 38.66 WATR ATOM 5397 OH2 WAT W 119 −5.862 6.629 4.446 1.00 39.57 WATR ATOM 5398 OH2 WAT W 120 14.133 −57.303 −28.159 1.00 30.19 WATR ATOM 5399 OH2 WAT W 121 −16.538 −6.724 21.638 1.00 40.50 WATR ATOM 5400 OH2 WAT W 122 19.669 −18.487 −33.216 1.00 38.38 WATR ATOM 5401 OH2 WAT W 123 15.481 1.078 −4.048 1.00 32.28 WATR ATOM 5402 OH2 WAT W 124 20.395 −13.033 −2.072 1.00 49.69 WATR ATOM 5403 OH2 WAT W 125 15.526 −1.437 −15.842 1.00 36.06 WATR ATOM 5404 OH2 WAT W 126 7.297 −29.419 −1.509 1.00 34.75 WATR ATOM 5405 OH2 WAT W 127 9.994 −12.069 −21.013 1.00 32.21 WATR ATOM 5406 OH2 WAT W 128 17.433 −42.825 −16.713 1.00 31.02 WATR ATOM 5407 OH2 WAT W 129 −15.855 20.882 21.019 1.00 44.11 WATR ATOM 5408 OH2 WAT W 130 −6.351 −7.687 −14.067 1.00 35.04 WATR ATOM 5409 OH2 WAT W 131 7.954 −17.872 −1.475 1.00 28.45 WATR ATOM 5410 OH2 WAT W 132 13.526 −34.593 −31.844 1.00 31.12 WATR ATOM 5411 OH2 WAT W 133 9.992 −41.228 −23.098 1.00 26.45 WATR ATOM 5412 OH2 WAT W 134 8.434 18.132 16.019 1.00 32.97 WATR ATOM 5413 OH2 WAT W 135 −1.208 −33.658 −36.216 1.00 38.33 WATR ATOM 5414 OH2 WAT W 136 −14.502 9.100 12.433 1.00 43.21 WATR ATOM 5415 OH2 WAT W 137 14.394 −43.675 − 17.325 1.00 32.32 WATR ATOM 5416 OH2 WAT W 138 −4.809 −30.333 −46.416 1.00 42.65 WATR ATOM 5417 OH2 WAT W 139 18.861 −35.072 −35.671 1.00 43.56 WATR ATOM 5418 OH2 WAT W 140 −10.162 −60.139 −32.862 1.00 35.41 WATR ATOM 5419 OH2 WAT W 141 6.740 −32.411 −35.303 1.00 38.57 WATR ATOM 5420 OH2 WAT W 142 −12.257 −60.854 −39.307 1.00 32.90 WATR ATOM 5421 OH2 WAT W 143 18.910 −40.984 − 13.084 1.00 43.43 WATR ATOM 5422 OH2 WAT W 144 18.857 −49.375 −28.645 1.00 31.34 WATR ATOM 5423 OH2 WAT W 145 0.235 −17.424 − 16.608 1.00 38.85 WATR ATOM 5424 OH2 WAT W 146 14.236 −11.252 −24.086 1.00 27.79 WATR ATOM 5425 OH2 WAT W 147 31.513 −22.336 −22.128 1.00 43.18 WATR ATOM 5426 OH2 WAT W 148 −5.314 −70.396 −26.090 1.00 43.91 WATR ATOM 5427 OH2 WAT W 149 −7.717 −64.969 −36.808 1.00 26.30 WATR ATOM 5428 OH2 WAT W 150 22.584 −12.594 −4.179 1.00 46.91 WATR ATOM 5429 OH2 WAT W 151 −12.388 9.493 36.619 1.00 32.82 WATR ATOM 5430 OH2 WAT W 152 −14.517 16.479 37.760 1.00 39.52 WATR ATOM 5431 OH2 WAT W 153 −10.095 −34.647 −29.068 1.00 41.08 WATR ATOM 5432 OH2 WAT W 154 −5.233 −4.134 31.160 1.00 35.31 WATR ATOM 5433 OH2 WAT W 155 −6.322 11.278 −1.883 1.00 35.75 WATR ATOM 5434 OH2 WAT W 156 10.262 −9.572 −16.736 1.00 42.40 WATR ATOM 5435 OH2 WAT W 157 22.929 −10.414 −23.566 1.00 36.66 WATR ATOM 5436 OH2 WAT W 158 −15.987 3.994 16.559 1.00 37.22 WATR ATOM 5437 OH2 WAT W 159 13.385 −44.923 −46.826 1.00 41.55 WATR ATOM 5438 OH2 WAT W 160 26.508 −13.616 −18.049 1.00 25.93 WATR ATOM 5439 OH2 WAT W 161 4.671 −66.907 −17.861 1.00 31.54 WATR ATOM 5440 OH2 WAT W 162 −12.589 12.262 11.825 1.00 32.71 WATR ATOM 5441 OH2 WAT W 163 13.899 −62.269 −25.144 1.00 30.71 WATR ATOM 5442 OH2 WAT W 164 −31.053 15.663 19.272 1.00 30.19 WATR ATOM 5443 OH2 WAT W 165 9.797 −47.899 −25.140 1.00 26.79 WATR ATOM 5444 OH2 WAT W 166 0.877 −51.774 −25.619 1.00 30.02 WATR ATOM 5445 OH2 WAT W 167 −17.088 16.246 37.180 1.00 25.63 WATR ATOM 5446 OH2 WAT W 168 0.855 −52.086 −22.078 1.00 40.99 WATR ATOM 5447 OH2 WAT W 169 −14.873 18.295 21.203 1.00 40.28 WATR ATOM 5448 OH2 WAT W 170 11.913 −62.134 −35.641 1.00 41.33 WATR ATOM 5449 OH2 WAT W 171 25.783 −23.984 −33.162 1.00 44.03 WATR ATOM 5450 OH2 WAT W 172 7.169 −50.047 −23.737 1.00 47.85 WATR ATOM 5451 OH2 WAT W 173 20.074 −42.845 −14.939 1.00 32.87 WATR ATOM 5452 OH2 WAT W 174 8.765 5.909 9.193 1.00 34.30 WATR ATOM 5453 OH2 WAT W 175 −4.953 −64.494 −45.351 1.00 47.11 WATR ATOM 5454 OH2 WAT W 176 11.889 −61.263 −22.531 1.00 36.63 WATR ATOM 5455 OH2 WAT W 177 2.149 −49.169 −24.836 1.00 39.21 WATR ATOM 5456 OH2 WAT W 178 −14.051 6.399 13.353 1.00 39.89 WATR ATOM 5457 OH2 WAT W 179 8.488 −46.760 −23.118 1.00 45.24 WATR ATOM 5458 OH2 WAT W 180 −1.152 −23.348 −11.975 1.00 30.36 WATR ATOM 5459 OH2 WAT W 181 −7.002 3.531 7.051 1.00 44.50 WATR ATOM 5460 OH2 WAT W 182 −12.320 −54.772 −29.990 1.00 38.61 WATR ATOM 5461 OH2 WAT W 183 6.790 −54.559 −47.733 1.00 44.05 WATR ATOM 5462 OH2 WAT W 184 26.305 −38.240 −19.177 1.00 39.53 WATR ATOM 5463 OH2 WAT W 185 20.402 −58.179 −34.391 1.00 46.11 WATR ATOM 5464 OH2 WAT W 186 8.061 −31.341 −19.653 1.00 41.37 WATR ATOM 5465 OH2 WAT W 187 −7.549 −15.619 −5.482 1.00 40.60 WATR ATOM 5466 OH2 WAT W 188 −31.099 11.941 25.471 1.00 38.80 WATR ATOM 5467 OH2 WAT W 189 28.566 −25.441 −15.103 1.00 34.75 WATR ATOM 5468 OH2 WAT W 190 −5.613 −40.109 −50.158 1.00 49.21 WATR ATOM 5469 OH2 WAT W 191 17.024 −13.428 1.709 1.00 39.93 WATR ATOM 5470 OH2 WAT W 192 −22.114 10.176 37.673 1.00 32.53 WATR ATOM 5471 OH2 WAT W 193 10.204 −29.330 −20.066 1.00 27.24 WATR ATOM 5472 OH2 WAT W 194 27.893 −25.793 −21.862 1.00 38.97 WATR ATOM 5473 OH2 WAT W 195 −5.582 17.681 32.898 1.00 43.64 WATR ATOM 5474 OH2 WAT W 196 23.004 −45.224 −27.870 1.00 43.04 WATR ATOM 5475 OH2 WAT W 197 5.189 −58.857 −25.016 1.00 28.15 WATR ATOM 5476 OH2 WAT W 198 −7.740 −56.165 −24.052 1.00 35.98 WATR ATOM 5477 OH2 WAT W 199 −8.156 24.723 26.733 1.00 45.54 WATR ATOM 5478 OH2 WAT W 200 23.286 −32.333 −33.400 1.00 38.12 WATR ATOM 5479 OH2 WAT W 201 30.646 −14.180 −20.528 1.00 31.01 WATR ATOM 5480 OH2 WAT W 202 −8.238 −4.609 29.299 1.00 39.76 WATR ATOM 5481 OH2 WAT W 203 19.370 0.814 −7.532 1.00 35.83 WATR ATOM 5482 OH2 WAT W 204 0.885 −27.619 −1.442 1.00 47.04 WATR ATOM 5483 OH2 WAT W 205 16.084 −56.649 −26.382 1.00 45.97 WATR ATOM 5484 OH2 WAT W 206 −0.698 −19.360 −9.869 1.00 37.53 WATR ATOM 5485 OH2 WAT W 207 0.682 −14.985 −15.794 1.00 33.35 WATR ATOM 5486 OH2 WAT W 208 1.646 17.427 31.991 1.00 40.39 WATR ATOM 5487 OH2 WAT W 209 −21.611 1.533 20.359 1.00 31.04 WATR ATOM 5488 OH2 WAT W 210 −5.143 −55.137 −45.825 1.00 30.17 WATR ATOM 5489 OH2 WAT W 211 −9.645 13.045 37.660 1.00 42.93 WATR ATOM 5490 OH2 WAT W 212 22.096 −11.242 −30.224 1.00 48.12 WATR ATOM 5491 OH2 WAT W 213 −5.759 2.610 −15.984 1.00 41.67 WATR ATOM 5492 OH2 WAT W 214 −4.323 7.731 −7.331 1.00 37.92 WATR ATOM 5493 OH2 WAT W 215 −5.450 7.197 10.632 1.00 33.99 WATR ATOM 5494 OH2 WAT W 216 2.330 −32.635 −34.500 1.00 38.85 WATR ATOM 5495 OH2 WAT W 217 −26.827 16.219 13.451 1.00 38.12 WATR ATOM 5496 OH2 WAT W 218 −10.887 −51.427 −23.191 1.00 39.81 WATR ATOM 5497 OH2 WAT W 219 −9.020 19.746 −3.698 1.00 46.58 WATR ATOM 5498 OH2 WAT W 220 9.054 6.622 −0.709 1.00 34.14 WATR ATOM 5499 OH2 WAT W 221 4.173 −7.985 −23.786 1.00 32.75 WATR ATOM 5500 OH2 WAT W 222 0.983 16.806 3.910 1.00 40.83 WATR ATOM 5501 OH2 WAT W 223 2.222 −16.848 −6.783 1.00 33.50 WATR ATOM 5502 OH2 WAT W 224 13.627 1.072 −15.114 1.00 37.51 WATR ATOM 5503 OH2 WAT W 225 12.533 −14.212 −9.007 1.00 38.40 WATR ATOM 5504 OH2 WAT W 226 1.404 −7.852 5.396 1.00 38.55 WATR ATOM 5505 OH2 WAT W 227 31.159 −24.354 −31.143 1.00 37.67 WATR ATOM 5506 OH2 WAT W 228 −13.047 −60.728 −42.282 1.00 42.18 WATR ATOM 5507 OH2 WAT W 229 8.956 −37.681 −16.765 1.00 41.45 WATR ATOM 5508 OH2 WAT W 230 28.749 −13.637 −16.860 1.00 42.34 WATR ATOM 5509 OH2 WAT W 231 −4.461 19.451 8.684 1.00 36.17 WATR ATOM 5510 OH2 WAT W 232 −9.785 −66.504 −35.701 1.00 44.07 WATR ATOM 5511 OH2 WAT W 233 10.673 −41.619 −20.678 1.00 36.58 WATR ATOM 5512 OH2 WAT W 234 −15.694 1.684 32.613 1.00 44.04 WATR ATOM 5513 OH2 WAT W 235 3.345 1.229 9.738 1.00 35.70 WATR ATOM 5514 OH2 WAT W 236 −6.256 −68.913 −30.401 1.00 36.72 WATR ATOM 5515 OH2 WAT W 237 28.344 −21.326 −30.399 1.00 36.45 WATR ATOM 5516 OH2 WAT W 238 2.876 −34.368 −17.344 1.00 42.48 WATR ATOM 5517 OH2 WAT W 239 15.355 −11.202 2.371 1.00 38.84 WATR ATOM 5518 OH2 WAT W 240 27.066 −22.336 −6.437 1.00 37.37 WATR ATOM 5519 OH2 WAT W 241 2.222 18.464 26.994 1.00 35.75 WATR ATOM 5520 OH2 WAT W 242 15.052 −9.829 −31.019 1.00 44.31 WATR ATOM 5521 OH2 WAT W 243 10.351 −67.649 −21.184 1.00 35.79 WATR ATOM 5522 OH2 WAT W 244 −13.173 14.269 38.605 1.00 41.50 WATR ATOM 5523 OH2 WAT W 245 −7.569 9.658 0.793 1.00 37.62 WATR ATOM 5524 OH2 WAT W 246 −2.167 −47.395 −19.605 1.00 45.90 WATR ATOM 5525 OH2 WAT W 247 7.166 2.400 15.830 1.00 42.90 WATR ATOM 5526 OH2 WAT W 248 −11.231 −10.901 −10.057 1.00 45.28 WATR ATOM 5527 OH2 WAT W 249 5.684 −16.094 −26.796 1.00 44.76 WATR ATOM 5528 OH2 WAT W 250 −4.745 3.667 −18.932 1.00 46.20 WATR ATOM 5529 OH2 WAT W 251 −0.505 −22.136 −9.079 1.00 42.89 WATR ATOM 5530 OH2 WAT W 252 16.668 −37.987 −7.767 1.00 35.76 WATR ATOM 5531 OH2 WAT W 253 2.454 −18.256 −26.130 1.00 43.33 WATR ATOM 5532 OH2 WAT W 254 −8.367 −39.960 −21.638 1.00 43.07 WATR ATOM 5533 OH2 WAT W 255 15.642 7.805 9.633 1.00 47.78 WATR ATOM 5534 OH2 WAT W 256 13.660 −24.331 1.932 1.00 42.50 WATR ATOM 5535 OH2 WAT W 257 11.567 −6.104 −23.359 1.00 37.10 WATR ATOM 5536 OH2 WAT W 258 18.941 −16.698 0.528 1.00 40.97 WATR ATOM 5537 OH2 WAT W 259 −11.441 −63.514 −39.126 1.00 43.17 WATR ATOM 5538 OH2 WAT W 260 28.664 −39.605 −22.853 1.00 42.65 WATR ATOM 5539 OH2 WAT W 261 6.795 −6.961 31.114 1.00 38.28 WATR ATOM 5540 OH2 WAT W 262 7.077 −14.349 −24.858 1.00 41.00 WATR ATOM 5541 OH2 WAT W 263 −2.259 −48.991 −29.099 1.00 34.96 WATR ATOM 5542 OH2 WAT W 264 21.812 −44.128 −35.641 1.00 44.51 WATR ATOM 5543 OH2 WAT W 265 −27.570 4.389 13.296 1.00 48.63 WATR ATOM 5544 OH2 WAT W 266 13.573 −27.185 0.220 1.00 43.56 WATR ATOM 5545 OH2 WAT W 267 16.549 8.451 −13.582 1.00 44.84 WATR ATOM 5546 OH2 WAT W 268 −9.142 9.107 36.872 1.00 37.66 WATR ATOM 5547 OH2 WAT W 269 5.648 −11.797 −24.893 1.00 45.79 WATR ATOM 5548 OH2 WAT W 270 3.619 −14.850 −23.652 1.00 34.09 WATR ATOM 5549 OH2 WAT W 271 −8.129 −11.098 −16.064 1.00 39.37 WATR ATOM 5550 OH2 WAT W 272 −17.342 8.563 9.979 1.00 46.38 WATR ATOM 5551 OH2 WAT W 273 8.798 −36.348 −46.119 1.00 37.71 WATR ATOM 5552 OH2 WAT W 274 9.190 −10.509 −35.865 1.00 45.80 WATR ATOM 5553 OH2 WAT W 275 13.545 −13.441 3.898 1.00 42.83 WATR ATOM 5554 OH2 WAT W 276 −7.844 0.944 −2.560 1.00 46.27 WATR ATOM 5555 OH2 WAT W 277 0.478 −47.721 −55.170 1.00 46.25 WATR ATOM 5556 OH2 WAT W 278 24.658 −18.359 −11.005 1.00 36.33 WATR ATOM 5557 OH2 WAT W 279 −4.675 21.561 12.155 1.00 37.17 WATR ATOM 5558 OH2 WAT W 280 0.382 20.486 4.930 1.00 41.40 WATR ATOM 5559 OH2 WAT W 281 5.919 18.010 25.033 1.00 41.72 WATR ATOM 5560 OH2 WAT W 282 −2.987 −63.751 −22.983 1.00 43.76 WATR ATOM 5561 OH2 WAT W 283 8.990 −33.134 −17.898 1.00 40.17 WATR ATOM 5562 OH2 WAT W 284 0.155 −61.872 −48.384 1.00 49.87 WATR ATOM 5563 OH2 WAT W 285 −10.443 −56.965 −24.681 1.00 48.02 WATR ATOM 5564 OH2 WAT W 286 18.915 −33.048 −3.930 1.00 37.81 WATR ATOM 5565 OH2 WAT W 287 −16.181 11.706 12.277 1.00 41.77 WATR ATOM 5566 OH2 WAT W 288 7.197 7.180 10.953 1.00 46.19 WATR ATOM 5567 OH2 WAT W 289 31.934 −26.155 −26.053 1.00 38.77 WATR ATOM 5568 OH2 WAT W 290 −15.232 −0.248 −11.315 1.00 40.14 WATR ATOM 5569 OH2 WAT W 291 9.450 −27.963 −1.396 1.00 41.29 WATR ATOM 5570 OH2 WAT W 292 −1.800 13.139 −9.983 1.00 41.60 WATR ATOM 5571 OH2 WAT W 293 −7.766 5.988 9.798 1.00 40.11 WATR ATOM 5572 OH2 WAT W 294 7.973 4.338 14.321 1.00 39.97 WATR ATOM 5573 OH2 WAT W 295 23.449 −40.563 −27.347 1.00 40.59 WATR ATOM 5574 OH2 WAT W 296 −3.537 −28.260 −15.925 1.00 42.10 WATR ATOM 5575 OH2 WAT W 297 28.052 −32.620 −12.168 1.00 48.03 WATR ATOM 5576 OH2 WAT W 298 20.655 −43.315 −28.829 1.00 40.17 WATR ATOM 5577 S SO4 S 1 1.273 −70.953 −23.009 1.00 22.99 SO4 ATOM 5578 O1 SO4 S 1 1.720 −71.882 −24.053 1.00 21.18 SO4 ATOM 5579 O2 SO4 S 1 0.908 −69.659 −23.626 1.00 22.47 SO4 ATOM 5580 O3 SO4 S 1 2.337 −70.752 −22.018 1.00 23.88 SO4 ATOM 5581 O4 SO4 S 1 0.088 −71.522 −22.328 1.00 22.50 SO4 TEREND

TABLE 2 ATOMIC COORDINATES OF E. COLI MURG C-ALPHA BACKBONE ATOMS ATOM 2649 CA LYS B 7 −6.512 −45.403 −47.519 1.00 45.28 BBBB ATOM 2651 CA ARG B 8 −6.682 −47.303 −44.240 1.00 38.63 BBBB ATOM 2662 CA LEU B 9 −4.094 −47.039 −41.477 1.00 30.88 BBBB ATOM 2670 CA MET B 10 −4.048 −49.055 −38.275 1.00 26.66 BBBB ATOM 2678 CA VAL B 11 −1.982 −47.605 −35.449 1.00 23.16 BBBB ATOM 2685 CA MET B 12 −0.523 −49.707 −32.613 1.00 24.54 BBBB ATOM 2693 CA ALA B 13 0.508 −47.410 −29.752 1.00 29.43 BBBB ATOM 2698 CA GLY B 14 −0.513 −47.804 −26.120 1.00 33.82 BBBB ATOM 2702 CA GLY B 15 −0.700 −45.047 −23.536 1.00 36.08 BBBB ATOM 2706 CA THR B 16 1.920 −46.787 −21.421 1.00 38.51 BBBB ATOM 2713 CA GLY B 17 5.367 −45.567 −22.392 1.00 36.57 BBBB ATOM 2717 CA GLY B 18 3.631 −42.529 −23.872 1.00 33.48 BBBB ATOM 2721 CA HIS B 19 3.548 −43.865 −27.435 1.00 28.22 BBBB ATOM 2731 CA VAL B 20 −0.098 −42.894 −27.965 1.00 27.77 BBBB ATOM 2738 CA PHE B 21 0.517 −39.136 −28.160 1.00 29.00 BBBB ATOM 2750 CA PRO B 22 2.986 −39.252 −31.086 1.00 26.12 BBBB ATOM 2756 CA GLY B 23 0.787 −41.864 −32.752 1.00 25.07 BBBB ATOM 2760 CA LEU B 24 −2.201 −39.551 −32.401 1.00 25.32 BBBB ATOM 2768 CA ALA B 25 −0.197 −36.754 −34.013 1.00 25.94 BBBB ATOM 2773 CA VAL B 26 0.466 −38.955 −37.056 1.00 25.70 BBBB ATOM 2780 CA ALA B 27 −3.116 −40.222 −37.199 1.00 26.15 BBBB ATOM 2785 CA HIS B 28 −4.574 −36.702 −37.190 1.00 29.32 BBBB ATOM 2795 CA HIS B 29 −2.070 −35.623 −39.806 1.00 32.38 BBBB ATOM 2805 CA LEU B 30 −3.136 −38.417 −42.162 1.00 32.00 BBBB ATOM 2813 CA MET B 31 −6.849 −38.064 −41.424 1.00 34.91 BBBB ATOM 2821 CA ALA B 32 −6.510 −34.511 −42.722 1.00 37.55 BBBB ATOM 2826 CA GLN B 33 −5.182 −36.070 −45.938 1.00 38.24 BBBB ATOM 2835 CA GLY B 34 −8.305 −38.169 −46.353 1.00 35.75 BBBB ATOM 2839 CA TRP B 35 −7.016 −41.246 −44.508 1.00 34.58 BBBB ATOM 2853 CA GLN B 36 −9.175 −43.535 −42.402 1.00 35.40 BBBB ATOM 2862 CA VAL B 37 −7.417 −44.516 −39.184 1.00 34.16 BBBB ATOM 2869 CA ARG B 38 −8.219 −47.286 −36.730 1.00 31.56 BBBB ATOM 2880 CA TRP B 39 −6.456 −48.070 −33.471 1.00 27.41 BBBB ATOM 2894 CA LEU B 40 −5.200 −51.364 −32.026 1.00 24.71 BBBB ATOM 2902 CA GLY B 41 −4.691 −51.450 −28.257 1.00 23.47 BBBB ATOM 2906 CA THR B 42 −5.787 −53.141 −25.027 1.00 29.84 BBBB ATOM 2913 CA ALA B 43 −9.000 −52.595 −23.047 1.00 38.81 BBBB ATOM 2918 CA ASP B 44 −7.455 −51.942 −19.632 1.00 44.47 BBBB ATOM 2926 CA ARG B 45 −4.887 −49.367 −20.763 1.00 40.44 BBBB ATOM 2937 CA MET B 46 −4.881 −45.581 −21.249 1.00 36.33 BBBB ATOM 2945 CA GLU B 47 −5.458 −45.655 −25.029 1.00 31.79 BBBB ATOM 2954 CA ALA B 48 −8.821 −47.344 −24.414 1.00 32.58 BBBB ATOM 2959 CA ASP B 49 −10.143 −44.065 −23.009 1.00 35.60 BBBB ATOM 2967 CA LEU B 50 −8.026 −41.484 −24.840 1.00 33.49 BBBB ATOM 2975 CA VAL B 51 −8.299 −42.641 −28.449 1.00 32.68 BBBB ATOM 2983 CA PRO B 52 −12.111 −42.601 −28.453 1.00 34.43 BBBB ATOM 2989 CA LYS B 53 −11.998 −39.054 −27.064 1.00 36.73 BBBB ATOM 2998 CA HIS B 54 −10.116 −38.212 −30.259 1.00 34.62 BBBB ATOM 3008 CA GLY B 55 −12.938 −39.481 −32.447 1.00 35.34 BBBB ATOM 3012 CA ILE B 56 −10.909 −42.517 −33.514 1.00 33.81 BBBB ATOM 3020 CA GLU B 57 −12.228 −46.083 −33.467 1.00 34.16 BBBB ATOM 3029 CA ILE B 58 −10.217 −48.658 −31.553 1.00 31.38 BBBB ATOM 3037 CA ASP B 59 −10.039 −52.442 −31.720 1.00 31.09 BBBB ATOM 3045 CA PHE B 60 −8.809 −54.410 −28.713 1.00 30.32 BBBB ATOM 3056 CA ILE B 61 −6.832 −57.616 −28.269 1.00 28.55 BBBB ATOM 3064 CA ARG B 62 −5.709 −59.416 −25.133 1.00 30.76 BBBB ATOM 3075 CA ILE B 63 −2.036 −59.770 −24.231 1.00 31.38 BBBB ATOM 3083 CA SER B 64 −2.356 −60.520 −20.505 1.00 37.51 BBBB ATOM 3089 CA GLY B 65 0.679 −62.355 −19.199 1.00 37.13 BBBB ATOM 3093 CA LEU B 66 2.591 −61.413 −22.355 1.00 33.17 BBBB ATOM 3101 CA ARG B 67 3.671 −57.928 −21.277 1.00 30.90 BBBB ATOM 3112 CA GLY B 68 7.380 −57.427 −20.685 1.00 26.79 BBBB ATOM 3116 CA LYS B 69 8.238 −60.463 −22.796 1.00 23.93 BBBB ATOM 3125 CA GLY B 70 10.755 −60.229 −25.636 1.00 22.26 BBBB ATOM 3129 CA ILE B 71 10.357 −62.386 −28.762 1.00 23.55 BBBB ATOM 3137 CA LYS B 72 12.038 −65.491 −27.343 1.00 24.92 BBBB ATOM 3146 CA ALA B 73 9.839 −65.306 −24.233 1.00 21.18 BBBB ATOM 3151 CA LEU B 74 6.745 −64.762 −26.387 1.00 19.36 BBBB ATOM 3159 CA ILE B 75 7.434 −67.768 −28.601 1.00 21.18 BBBB ATOM 3167 CA ALA B 76 7.996 −69.726 −25.374 1.00 21.72 BBBB ATOM 3172 CA ALA B 77 4.289 −69.121 −24.655 1.00 21.07 BBBB ATOM 3178 CA PRO B 78 2.772 −70.846 −27.771 1.00 20.95 BBBB ATOM 3184 CA LEU B 79 −0.896 −70.728 −26.783 1.00 21.32 BBBB ATOM 3192 CA ARG B 80 −0.980 −67.115 −25.637 1.00 21.30 BBBB ATOM 3203 CA ILE B 81 1.113 −65.621 −28.421 1.00 19.47 BBBB ATOM 3211 CA PHE B 82 −0.875 −67.582 −31.038 1.00 19.15 BBBB ATOM 3222 CA ASN B 83 −4.150 −66.332 −29.577 1.00 20.90 BBBB ATOM 3230 CA ALA B 84 −3.177 −62.647 −29.484 1.00 19.30 BBBB ATOM 3235 CA TRP B 85 −1.820 −63.111 −33.032 1.00 20.56 BBBB ATOM 3249 CA ARG B 86 −5.140 −64.660 −34.166 1.00 23.28 BBBB ATOM 3260 CA GLN B 87 −7.101 −61.802 −32.567 1.00 24.07 BBBB ATOM 3269 CA ALA B 88 −4.996 −59.183 −34.355 1.00 23.78 BBBB ATOM 3274 CA ARG B 89 −5.285 −61.111 −37.636 1.00 24.94 BBBB ATOM 3285 CA ALA B 90 −9.088 −61.151 −37.383 1.00 26.16 BBBB ATOM 3290 CA ILE B 91 −9.108 −57.400 −36.733 1.00 26.97 BBBB ATOM 3298 CA MET B 92 −6.872 −56.693 −39.717 1.00 29.03 BBBB ATOM 3306 CA LYS B 93 −8.735 −59.038 −42.050 1.00 33.20 BBBB ATOM 3315 CA ALA B 94 −11.943 −57.157 −41.183 1.00 33.62 BBBB ATOM 3320 CA TYR B 95 −10.504 −53.620 −41.224 1.00 33.83 BBBB ATOM 3332 CA LYS B 96 −8.104 −54.327 −44.122 1.00 33.85 BBBB ATOM 3342 CA PRO B 97 −5.490 −51.623 −43.419 1.00 31.82 BBBB ATOM 3348 CA ASP B 98 −3.049 −50.685 −46.188 1.00 29.78 BBBB ATOM 3356 CA VAL B 99 −0.296 −50.214 −43.660 1.00 26.75 BBBB ATOM 3363 CA VAL B 100 0.227 −50.613 −39.936 1.00 23.59 BBBB ATOM 3370 CA LEU B 101 2.214 −48.199 −37.797 1.00 21.59 BBBB ATOM 3378 CA GLY B 102 3.796 −49.357 −34.549 1.00 19.23 BBBB ATOM 3382 CA MET B 103 4.892 −46.597 −32.191 1.00 18.93 BBBB ATOM 3390 CA GLY B 104 6.275 −49.080 −29.686 1.00 21.89 BBBB ATOM 3394 CA GLY B 105 4.593 −50.905 −26.827 1.00 23.54 BBBB ATOM 3398 CA TYR B 106 3.818 −54.554 −26.159 1.00 22.37 BBBB ATOM 3410 CA VAL B 107 0.557 −54.694 −28.099 1.00 18.06 BBBB ATOM 3417 CA SER B 108 2.488 −53.892 −31.290 1.00 19.67 BBBB ATOM 3423 CA GLY B 109 4.251 −57.256 −31.023 1.00 20.03 BBBB ATOM 3428 CA PRO B 110 1.251 −59.478 −31.855 1.00 18.99 BBBB ATOM 3434 CA GLY B 111 −0.160 −56.702 −34.025 1.00 19.60 BBBB ATOM 3438 CA GLY B 112 3.014 −56.417 −36.074 1.00 19.97 BBBB ATOM 3442 CA LEU B 113 3.265 −60.184 −36.429 1.00 19.49 BBBB ATOM 3450 CA ALA B 114 −0.334 −60.292 −37.661 1.00 18.70 BBBB ATOM 3455 CA ALA B 115 0.167 −57.516 −40.229 1.00 21.84 BBBB ATOM 3460 CA TRP B 116 3.365 −59.126 −41.478 1.00 23.22 BBBB ATOM 3474 CA SER B 117 1.735 −62.573 −41.873 1.00 22.61 BBBB ATOM 3480 CA LEU B 118 −1.069 −60.957 −43.882 1.00 25.70 BBBB ATOM 3488 CA GLY B 119 1.354 −59.174 −46.192 1.00 27.80 BBBB ATOM 3492 CA ILE B 120 0.568 −55.744 −44.731 1.00 24.85 BBBB ATOM 3501 CA PRO B 121 3.625 −53.477 −44.591 1.00 22.63 BBBB ATOM 3507 CA VAL B 122 4.743 −52.594 −41.083 1.00 22.03 BBBB ATOM 3514 CA VAL B 123 6.200 −49.184 −40.310 1.00 20.82 BBBB ATOM 3521 CA LEU B 124 7.749 −48.485 −36.915 1.00 22.10 BBBB ATOM 3529 CA HIS B 125 8.814 −45.413 −34.981 1.00 21.42 BBBB ATOM 3539 CA GLU B 126 10.947 −45.452 −31.817 1.00 22.15 BBBB ATOM 3548 CA GLN B 127 10.682 −42.270 −29.735 1.00 22.81 BBBB ATOM 3557 CA ASN B 128 13.406 −43.097 −27.216 1.00 22.96 BBBB ATOM 3565 CA GLY B 129 17.203 −43.019 −27.294 1.00 25.36 BBBB ATOM 3569 CA ILE B 130 17.160 −46.716 −26.488 1.00 28.00 BBBB ATOM 3577 CA ALA B 131 14.978 −49.139 −28.461 1.00 25.88 BBBB ATOM 3582 CA GLY B 132 12.007 −50.532 −26.568 1.00 24.05 BBBB ATOM 3586 CA LEU B 133 11.903 −54.293 −26.020 1.00 24.54 BBBB ATOM 3594 CA THR B 134 9.202 −54.860 −28.639 1.00 21.22 BBBB ATOM 3601 CA ASN B 135 10.407 −52.419 −31.324 1.00 20.50 BBBB ATOM 3609 CA LYS B 136 13.886 −53.949 −31.144 1.00 22.79 BBBB ATOM 3618 CA TRP B 137 12.753 −57.345 −32.424 1.00 22.06 BBBB ATOM 3632 CA LEU B 138 9.744 −56.188 −34.431 1.00 23.15 BBBB ATOM 3640 CA ALA B 139 12.128 −54.092 −36.542 1.00 25.29 BBBB ATOM 3645 CA LYS B 140 13.279 −57.337 −38.182 1.00 28.05 BBBB ATOM 3654 CA ILE B 141 9.963 −57.818 −40.016 1.00 26.09 BBBB ATOM 3662 CA ALA B 142 9.331 −54.107 −40.498 1.00 25.03 BBBB ATOM 3667 CA THR B 143 9.262 −52.595 −43.984 1.00 26.10 BBBB ATOM 3674 CA LYS B 144 10.436 −49.238 −42.618 1.00 24.73 BBBB ATOM 3683 CA VAL B 145 11.947 −48.311 −39.252 1.00 23.62 BBBB ATOM 3690 CA MET B 146 12.338 −44.736 −37.993 1.00 23.15 BBBB ATOM 3698 CA GLN B 147 13.762 −43.418 −34.712 1.00 25.05 BBBB ATOM 3707 CA ALA B 148 13.559 −40.032 −33.009 1.00 26.88 BBBB ATOM 3712 CA PHE B 149 17.239 −39.820 −32.098 1.00 29.39 BBBB ATOM 3724 CA PRO B 150 20.310 −41.541 −33.535 1.00 31.87 BBBB ATOM 3730 CA GLY B 151 21.629 −44.537 −31.595 1.00 32.62 BBBB ATOM 3734 CA ALA B 152 18.447 −46.476 −30.753 1.00 32.71 BBBB ATOM 3739 CA PHE B 153 18.925 −48.506 −33.937 1.00 34.83 BBBB ATOM 3751 CA PRO B 154 22.158 −48.751 −35.993 1.00 38.97 BBBB ATOM 3757 CA ASN B 155 20.765 −47.568 −39.346 1.00 41.08 BBBB ATOM 3765 CA ALA B 156 17.170 −46.407 −38.843 1.00 37.55 BBBB ATOM 3770 CA GLU B 157 16.367 −43.044 −40.460 1.00 34.40 BBBB ATOM 3779 CA VAL B 158 16.337 −40.344 −37.764 1.00 31.16 BBBB ATOM 3786 CA VAL B 159 13.155 −38.265 −37.889 1.00 28.10 BBBB ATOM 3793 CA GLY B 160 12.724 −36.921 −34.355 1.00 26.93 BBBB ATOM 3797 CA ASN B 161 9.456 −36.807 −32.375 1.00 25.27 BBBB ATOM 3806 CA PRO B 162 6.315 −34.747 −33.004 1.00 26.14 BBBB ATOM 3812 CA VAL B 163 6.456 −31.379 −31.216 1.00 27.75 BBBB ATOM 3819 CA ARG B 164 3.667 −28.953 −30.246 1.00 32.36 BBBB ATOM 3830 CA THR B 165 3.038 −26.307 −32.924 1.00 31.74 BBBB ATOM 3837 CA ASP B 166 3.252 −23.404 −30.466 1.00 30.64 BBBB ATOM 3845 CA VAL B 167 6.746 −24.503 −29.440 1.00 25.91 BBBB ATOM 3852 CA LEU B 168 7.780 −25.002 −33.075 1.00 28.46 BBBB ATOM 3860 CA ALA B 169 6.580 −21.455 −33.756 1.00 31.43 BBBB ATOM 3865 CA LEU B 170 9.002 −19.905 −31.268 1.00 29.60 BBBB ATOM 3874 CA PRO B 171 11.611 −17.457 −32.642 1.00 30.11 BBBB ATOM 3880 CA LEU B 172 15.157 −18.780 −33.062 1.00 28.33 BBBB ATOM 3889 CA PRO B 173 17.450 −18.550 −29.977 1.00 25.25 BBBB ATOM 3895 CA GLN B 174 19.526 −15.527 −31.049 1.00 25.46 BBBB ATOM 3904 CA GLN B 175 16.365 −13.525 −31.718 1.00 28.47 BBBB ATOM 3913 CA ARG B 176 14.611 −14.635 −28.525 1.00 29.01 BBBB ATOM 3924 CA LEU B 177 17.673 −13.970 −26.331 1.00 29.90 BBBB ATOM 3932 CA ALA B 178 18.766 −10.776 −28.131 1.00 30.78 BBBB ATOM 3937 CA GLY B 179 19.846 −7.993 −25.784 1.00 30.10 BBBB ATOM 3941 CA ARG B 180 18.676 −9.965 −22.787 1.00 28.97 BBBB ATOM 3952 CA GLU B 181 20.545 −9.027 −19.621 1.00 31.79 BBBB ATOM 3961 CA GLY B 182 19.871 −9.586 −15.943 1.00 27.75 BBBB ATOM 3966 CA PRO B 183 19.450 −12.832 −13.913 1.00 22.93 BBBB ATOM 3972 CA VAL B 184 19.524 −16.146 −15.729 1.00 18.01 BBBB ATOM 3979 CA ARG B 185 15.873 −17.216 −16.011 1.00 17.62 BBBB ATOM 3990 CA VAL B 186 15.508 −20.771 −14.741 1.00 16.47 BBBB ATOM 3997 CA LEU B 187 12.361 −22.710 −15.604 1.00 16.75 BBBB ATOM 4005 CA VAL B 188 11.774 −25.775 −13.381 1.00 18.41 BBBB ATOM 4012 CA VAL B 189 9.298 −28.234 −14.948 1.00 22.11 BBBB ATOM 4019 CA GLY B 190 7.914 −31.188 −12.994 1.00 27.28 BBBB ATOM 4023 CA GLY B 191 4.935 −32.163 −15.115 1.00 31.94 BBBB ATOM 4027 CA SER B 192 1.313 −32.665 −14.064 1.00 35.91 BBBB ATOM 4033 CA GLN B 193 2.292 −34.763 −11.033 1.00 38.53 BBBB ATOM 4042 CA GLY B 194 5.398 −32.711 −10.350 1.00 35.02 BBBB ATOM 4046 CA ALA B 195 8.977 −33.819 −9.709 1.00 33.12 BBBB ATOM 4051 CA ARG B 196 9.538 −34.512 −6.010 1.00 32.63 BBBB ATOM 4062 CA ILE B 197 13.329 −34.168 −6.164 1.00 28.10 BBBB ATOM 4070 CA LEU B 198 13.069 −30.833 −8.003 1.00 26.58 BBBB ATOM 4078 CA ASN B 199 10.497 −29.447 −5.563 1.00 27.07 BBBB ATOM 4086 CA GLN B 200 12.955 −30.326 −2.794 1.00 30.10 BBBB ATOM 4095 CA THR B 201 16.215 −29.345 −4.474 1.00 27.34 BBBB ATOM 4102 CA MET B 202 15.567 −26.048 −6.268 1.00 23.68 BBBB ATOM 4111 CA PRO B 203 14.608 −23.963 −3.220 1.00 23.84 BBBB ATOM 4117 CA GLN B 204 18.033 −24.708 −1.684 1.00 26.34 BBBB ATOM 4126 CA VAL B 205 19.672 −24.033 −5.043 1.00 24.44 BBBB ATOM 4133 CA ALA B 206 17.980 −20.610 −5.013 1.00 22.84 BBBB ATOM 4138 CA ALA B 207 19.442 −19.857 −1.576 1.00 26.65 BBBB ATOM 4143 CA LYS B 208 22.915 −20.595 −2.919 1.00 28.31 BBBB ATOM 4152 CA LEU B 209 22.577 −18.640 −6.171 1.00 25.68 BBBB ATOM 4160 CA GLY B 210 20.675 −15.628 −4.804 1.00 26.56 BBBB ATOM 4164 CA ASP B 211 20.370 −12.647 −7.190 1.00 28.28 BBBB ATOM 4172 CA SER B 212 22.098 −14.474 −10.067 1.00 25.73 BBBB ATOM 4178 CA VAL B 213 18.925 −16.308 −11.116 1.00 20.76 BBBB ATOM 4185 CA THR B 214 15.204 −15.726 −11.337 1.00 19.60 BBBB ATOM 4192 CA ILE B 215 13.076 −18.850 −11.169 1.00 18.75 BBBB ATOM 4200 CA TRP B 216 9.661 −19.973 −12.378 1.00 19.34 BBBB ATOM 4214 CA HIS B 217 9.015 −23.303 −10.680 1.00 21.06 BBBB ATOM 4224 CA GLN B 218 6.149 −25.594 −11.735 1.00 24.30 BBBB ATOM 4233 CA SER B 219 5.463 −27.800 −8.684 1.00 26.73 BBBB ATOM 4239 CA GLY B 220 2.855 −30.242 −9.961 1.00 30.53 BBBB ATOM 4243 CA LYS B 221 −0.657 −30.914 −8.628 1.00 35.12 BBBB ATOM 4252 CA GLY B 222 −1.195 −29.899 −5.011 1.00 35.34 BBBB ATOM 4256 CA SER B 223 2.451 −28.934 −4.418 1.00 33.98 BBBB ATOM 4262 CA GLN B 224 2.187 −25.208 −5.186 1.00 33.71 BBBB ATOM 4271 CA GLN B 225 1.823 −24.239 −1.519 1.00 32.32 BBBB ATOM 4280 CA SER B 226 4.701 −26.309 −0.122 1.00 28.30 BBBB ATOM 4286 CA VAL B 227 7.214 −25.247 −2.791 1.00 24.28 BBBB ATOM 4293 CA GLU B 228 6.178 −21.592 −2.387 1.00 27.23 BBBB ATOM 4302 CA GLN B 229 6.853 −22.046 1.329 1.00 28.38 BBBB ATOM 4311 CA ALA B 230 10.185 −23.754 0.682 1.00 26.18 BBBB ATOM 4316 CA TYR B 231 11.371 −20.766 −1.366 1.00 25.47 BBBB ATOM 4328 CA ALA B 232 10.342 −18.322 1.368 1.00 27.51 BBBB ATOM 4333 CA GLU B 233 12.145 −20.441 3.966 1.00 30.87 BBBB ATOM 4342 CA ALA B 234 15.215 −20.417 1.714 1.00 28.48 BBBB ATOM 4347 CA GLY B 235 15.033 −16.627 1.815 1.00 26.23 BBBB ATOM 4351 CA GLN B 236 14.121 −16.198 −1.870 1.00 25.53 BBBB ATOM 4361 CA PRO B 237 10.336 −15.587 −1.720 1.00 24.65 BBBB ATOM 4367 CA GLN B 238 10.277 −13.558 −4.945 1.00 24.29 BBBB ATOM 4376 CA HIS B 239 10.526 −16.608 −7.201 1.00 22.08 BBBB ATOM 4386 CA LYS B 240 7.375 −17.589 −9.105 1.00 23.26 BBBB ATOM 4395 CA VAL B 241 5.740 −20.911 −8.277 1.00 23.78 BBBB ATOM 4402 CA THR B 242 2.758 −22.301 −10.177 1.00 25.93 BBBB ATOM 4409 CA GLU B 243 0.999 −25.651 −9.837 1.00 27.03 BBBB ATOM 4418 CA PHE B 244 0.964 −26.068 −13.620 1.00 26.54 BBBB ATOM 4429 CA ILE B 245 1.932 −24.242 −16.802 1.00 28.48 BBBB ATOM 4437 CA ASP B 246 −0.754 −24.396 −19.457 1.00 36.00 BBBB ATOM 4445 CA ASP B 247 1.245 −22.392 −21.999 1.00 30.74 BBBB ATOM 4453 CA MET B 248 4.625 −24.136 −22.138 1.00 28.41 BBBB ATOM 4461 CA ALA B 249 5.512 −22.216 −25.290 1.00 24.67 BBBB ATOM 4466 CA ALA B 250 5.188 −18.933 −23.390 1.00 21.78 BBBB ATOM 4471 CA ALA B 251 7.301 −20.259 −20.501 1.00 20.85 BBBB ATOM 4476 CA TYR B 252 9.972 −21.616 −22.886 1.00 22.78 BBBB ATOM 4488 CA ALA B 253 10.131 −18.224 −24.636 1.00 23.54 BBBB ATOM 4493 CA TRP B 254 10.829 −16.534 −21.303 1.00 19.76 BBBB ATOM 4507 CA ALA B 255 13.399 −19.025 −20.003 1.00 19.51 BBBB ATOM 4512 CA ASP B 256 17.176 −19.026 −20.434 1.00 17.58 BBBB ATOM 4520 CA VAL B 257 17.535 −22.603 −19.194 1.00 18.53 BBBB ATOM 4527 CA VAL B 258 15.208 −25.456 −18.234 1.00 19.32 BBBB ATOM 4534 CA VAL B 259 15.581 −27.957 −15.374 1.00 19.85 BBBB ATOM 4541 CA CYS B 260 13.454 −31.055 −15.946 1.00 22.00 BBBB ATOM 4547 CA ARG B 261 13.170 −34.800 −16.515 1.00 23.75 BBBB ATOM 4558 CA SER B 262 13.975 −36.189 −19.948 1.00 23.18 BBBB ATOM 4564 CA GLY B 263 11.026 −38.079 −21.361 1.00 22.85 BBBB ATOM 4568 CA ALA B 264 11.482 −38.564 −25.115 1.00 24.25 BBBB ATOM 4573 CA LEU B 265 8.846 −36.037 −26.205 1.00 24.66 BBBB ATOM 4581 CA THR B 266 10.194 −33.557 −23.657 1.00 22.34 BBBB ATOM 4588 CA VAL B 267 13.730 −33.762 −25.023 1.00 21.11 BBBB ATOM 4595 CA SER B 268 12.411 −33.191 −28.567 1.00 21.96 BBBB ATOM 4601 CA GLU B 269 10.282 −30.272 −27.378 1.00 21.95 BBBB ATOM 4610 CA ILE B 270 13.295 −28.698 −25.638 1.00 20.62 BBBB ATOM 4618 CA ALA B 271 15.440 −29.058 −28.776 1.00 22.45 BBBB ATOM 4623 CA ALA B 272 12.719 −27.451 −30.898 1.00 22.17 BBBB ATOM 4628 CA ALA B 273 12.361 −24.596 −28.407 1.00 21.97 BBBB ATOM 4633 CA GLY B 274 16.093 −24.023 −28.709 1.00 21.07 BBBB ATOM 4637 CA LEU B 275 16.666 −24.057 −24.966 1.00 19.78 BBBB ATOM 4646 CA PRO B 276 19.651 −25.199 −22.875 1.00 16.62 BBBB ATOM 4652 CA ALA B 277 18.638 −27.807 −20.321 1.00 15.80 BBBB ATOM 4657 CA LEU B 278 19.896 −29.429 −17.145 1.00 18.48 BBBB ATOM 4665 CA PHE B 279 18.266 −32.838 −17.392 1.00 21.59 BBBB ATOM 4676 CA VAL B 280 17.502 −34.902 −14.281 1.00 25.67 BBBB ATOM 4684 CA PRO B 281 16.698 −38.320 −15.824 1.00 29.05 BBBB ATOM 4690 CA PHE B 282 14.246 −40.496 −13.926 1.00 37.13 BBBB ATOM 4701 CA GLN B 283 16.319 −43.395 −12.591 1.00 41.11 BBBB ATOM 4710 CA HIS B 284 15.641 −46.917 −13.843 1.00 43.69 BBBB ATOM 4720 CA LYS B 285 17.767 −49.993 −14.571 1.00 45.34 BBBB ATOM 4729 CA ASP B 286 16.949 −49.299 −18.222 1.00 43.26 BBBB ATOM 4737 CA ARG B 287 17.951 −45.623 −17.883 1.00 36.28 BBBB ATOM 4748 CA GLN B 288 15.622 −44.804 −20.755 1.00 30.77 BBBB ATOM 4757 CA GLN B 289 15.474 −41.099 −19.904 1.00 29.46 BBBB ATOM 4766 CA TYR B 290 19.228 −40.984 −19.550 1.00 29.55 BBBB ATOM 4778 CA TRP B 291 19.542 −42.282 −23.116 1.00 28.07 BBBB ATOM 4792 CA ASN B 292 16.902 −39.784 −24.270 1.00 26.06 BBBB ATOM 4800 CA ALA B 293 18.926 −36.822 −22.979 1.00 25.69 BBBB ATOM 4805 CA LEU B 294 22.354 −38.088 −24.032 1.00 25.90 BBBB ATOM 4814 CA PRO B 295 21.998 −36.870 −27.635 1.00 26.15 BBBB ATOM 4820 CA LEU B 296 21.521 −33.265 −26.481 1.00 25.42 BBBB ATOM 4828 CA GLU B 297 24.354 −33.530 −23.953 1.00 28.78 BBBB ATOM 4837 CA LYS B 298 26.644 −34.947 −26.648 1.00 31.90 BBBB ATOM 4846 CA ALA B 299 25.773 −31.965 −28.847 1.00 30.38 BBBB ATOM 4851 CA GLY B 300 26.777 −29.635 −26.017 1.00 26.18 BBBB ATOM 4855 CA ALA B 301 23.214 −28.333 −25.638 1.00 22.50 BBBB ATOM 4860 CA ALA B 302 22.516 −29.770 −22.186 1.00 21.78 BBBB ATOM 4865 CA LYS B 303 23.979 −31.340 −19.048 1.00 25.86 BBBB ATOM 4874 CA ILE B 304 22.753 −34.598 −17.550 1.00 27.17 BBBB ATOM 4882 CA ILE B 305 22.843 −35.178 −13.813 1.00 29.01 BBBB ATOM 4890 CA GLU B 306 21.664 −38.702 −13.061 1.00 34.65 BBBB ATOM 4899 CA GLN B 307 20.377 −39.599 −9.613 1.00 40.54 BBBB ATOM 4909 CA PRO B 308 23.828 −40.891 −8.484 1.00 43.20 BBBB ATOM 4915 CA GLN B 309 25.247 −37.361 −8.787 1.00 43.46 BBBB ATOM 4924 CA LEU B 310 22.232 −35.166 −8.022 1.00 39.65 BBBB ATOM 4932 CA SER B 311 22.660 −32.714 −5.154 1.00 34.90 BBBB ATOM 4938 CA VAL B 312 21.990 −29.074 −4.341 1.00 31.50 BBBB ATOM 4945 CA ASP B 313 25.642 −28.202 −4.957 1.00 29.61 BBBB ATOM 4953 CA ALA B 314 25.782 −30.099 −8.254 1.00 26.47 BBBB ATOM 4958 CA VAL B 315 22.755 −28.215 −9.612 1.00 25.33 BBBB ATOM 4965 CA ALA B 316 23.888 −24.872 −8.199 1.00 27.13 BBBB ATOM 4970 CA ASN B 317 27.444 −25.246 −9.518 1.00 28.52 BBBB ATOM 4978 CA THR B 318 26.174 −26.371 −12.906 1.00 27.04 BBBB ATOM 4985 CA LEU B 319 23.883 −23.370 −13.357 1.00 25.21 BBBB ATOM 4993 CA ALA B 320 26.445 −20.931 −11.957 1.00 24.59 BBBB ATOM 4998 CA GLY B 321 28.934 −22.031 −14.591 1.00 24.34 BBBB ATOM 5002 CA TRP B 322 26.738 −21.007 −17.521 1.00 21.72 BBBB ATOM 5016 CA SER B 323 27.141 −17.404 −18.692 1.00 19.04 BBBB ATOM 5022 CA ARG B 324 24.725 −15.741 −21.112 1.00 18.09 BBBB ATOM 5033 CA GLU B 325 27.220 −16.368 −23.954 1.00 16.96 BBBB ATOM 5042 CA THR B 326 27.460 −20.055 −23.070 1.00 16.39 BBBB ATOM 5049 CA LEU B 327 23.659 −20.305 −22.780 1.00 17.27 BBBB ATOM 5057 CA LEU B 328 23.175 −18.745 −26.222 1.00 17.39 BBBB ATOM 5065 CA THR B 329 25.567 −21.335 −27.688 1.00 21.30 BBBB ATOM 5072 CA MET B 330 23.771 −24.153 −25.870 1.00 19.91 BBBB ATOM 5080 CA ALA B 331 20.412 −22.871 −27.098 1.00 18.49 BBBB ATOM 5085 CA GLU B 332 21.626 −22.827 −30.704 1.00 21.47 BBBB ATOM 5094 CA ARG B 333 23.040 −26.330 −30.408 1.00 23.77 BBBB ATOM 5105 CA ALA B 334 19.648 −27.420 −29.063 1.00 22.88 BBBB ATOM 5110 CA ARG B 335 17.795 −25.892 −32.002 1.00 23.54 BBBB ATOM 5121 CA ALA B 336 20.330 −27.477 −34.372 1.00 26.85 BBBB ATOM 5126 CA ALA B 337 19.740 −30.925 −32.865 1.00 30.89 BBBB ATOM 5131 CA SER B 338 16.008 −30.432 −33.408 1.00 32.41 BBBB ATOM 5137 CA ILE B 339 13.882 −31.941 −36.187 1.00 34.35 BBBB ATOM 5146 CA PRO B 340 10.733 −29.730 −36.600 1.00 34.94 BBBB ATOM 5152 CA ASP B 341 8.711 −31.820 −39.056 1.00 33.33 BBBB ATOM 5160 CA ALA B 342 8.875 −35.238 −37.411 1.00 29.09 BBBB ATOM 5165 CA THR B 343 5.115 −35.696 −37.744 1.00 28.55 BBBB ATOM 5172 CA GLU B 344 5.085 −34.933 −41.480 1.00 32.00 BBBB ATOM 5181 CA ARG B 345 8.138 −37.123 −42.067 1.00 31.44 BBBB ATOM 5192 CA VAL B 346 6.578 −40.151 −40.384 1.00 28.61 BBBB ATOM 5199 CA ALA B 347 3.249 −39.617 −42.137 1.00 28.96 BBBB ATOM 5204 CA ASN B 348 5.035 −39.286 −45.493 1.00 34.56 BBBB ATOM 5212 CA GLU B 349 6.954 −42.540 −44.956 1.00 34.86 BBBB ATOM 5221 CA VAL B 350 3.767 −44.306 −43.919 1.00 33.79 BBBB ATOM 5228 CA SER B 351 2.196 −42.946 −47.095 1.00 36.67 BBBB ATOM 5234 CA ARG B 352 5.114 −44.088 −49.251 1.00 40.03 BBBB ATOM 5245 CA VAL B 353 5.089 −47.587 −47.737 1.00 42.78 BBBB ATOM 5252 CA ALA B 354 1.336 −47.957 −48.212 1.00 47.24 BBBB ATOM 5257 CA ARG B 355 2.035 −46.964 −51.824 1.00 52.71 BBBB ATOM 5268 CA ALA B 356 4.453 −49.913 −51.809 1.00 54.93 BBBB ATOM 5273 CA LEU B 357 7.023 −47.522 −53.289 1.00 57.81 BBBB END

TABLE 3 ATOMIC COORDINATES OF E. COLI MURG C-ALPHA BACKBONE AND CONSERVED AMINO ACID RESIDUES ATOM 2649 CA LYS B 7 −6.512 −45.403 −47.519 1.00 45.23 BBBB ATOM 2651 CA ARG B 8 −6.682 −47.303 −44.240 1.00 38.63 BBBB ATOM 2662 CA LEU B 9 −4.094 −47.039 −41.477 1.00 30.88 BBBB ATOM 2670 CA MET B 10 −4.048 −49.055 −38.275 1.00 26.66 BBBB ATOM 2678 CA VAL B 11 −1.982 −47.605 −35.449 1.00 23.16 BBBB ATOM 2685 CA MET B 12 −0.523 −49.707 −32.613 1.00 24.54 BBBB ATOM 2693 CA ALA B 13 0.508 −47.410 −29.752 1.00 29.43 BBBB ATOM 2697 N GLY B 14 0.150 −47.934 −27.405 1.00 32.46 BBBB ATOM 2698 CA GLY B 14 −0.513 −47.804 −26.120 1.00 33.82 BBBB ATOM 2699 C GLY B 14 −0.107 −46.595 −25.299 1.00 34.82 BBBB ATOM 2700 O GLY B 14 0.975 −46.040 −25.479 1.00 35.47 BBBB ATOM 2701 N GLY B 15 −0.986 −46.188 −24.385 1.00 35.56 BBBB ATOM 2702 CA GLY B 15 −0.700 −45.047 −23.536 1.00 36.08 BBBB ATOM 2703 C GLY B 15 0.539 −45.254 −22.683 1.00 36.84 BBBB ATOM 2704 O GLY B 15 1.293 −44.311 −22.426 1.00 36.03 BBBB ATOM 2706 CA THR B 16 1.920 −46.787 −21.421 1.00 38.51 BBBB ATOM 2713 CA GLY B 17 5.367 −45.567 −22.392 1.00 36.57 BBBB ATOM 2716 N GLY B 18 3.949 −43.752 −23.150 1.00 33.83 BBBB ATOM 2717 CA GLY B 18 3.631 −42.529 −23.872 1.00 33.48 BBBB ATOM 2718 C GLY B 18 3.825 −42.593 −25.378 1.00 33.12 BBBB ATOM 2719 O GLY B 18 4.345 −41.650 −25.984 1.00 35.38 BBBB ATOM 2720 N HIS B 19 3.416 −43.699 −25.988 1.00 30.26 BBBB ATOM 2721 CA HIS B 19 3.548 −43.865 −27.435 1.00 28.22 BBBB ATOM 2722 CB HIS B 19 3.772 −45.349 −27.779 1.00 25.81 BBBB ATOM 2723 CG HIS B 19 4.957 −45.966 −27.094 1.00 25.35 BBBB ATOM 2724 CD2 HIS B 19 6.281 −45.694 −27.184 1.00 24.18 BBBB ATOM 2725 ND1 HIS B 19 4.845 −47.025 −26.217 1.00 24.57 BBBB ATOM 2726 CE1 HIS B 19 6.046 −47.380 −25.798 1.00 23.08 BBBB ATOM 2727 NE2 HIS B 19 6.936 −46.589 −26.369 1.00 25.51 BBBB ATOM 2728 C HIS B 19 2.280 −43.370 −28.144 1.00 27.91 BBBB ATOM 2729 O HIS B 19 2.300 −43.049 −29.337 1.00 26.91 BBBB ATOM 2731 CA VAL B 20 −0.098 −42.894 −27.965 1.00 27.77 BBBB ATOM 2738 CA PHE B 21 0.517 −39.136 −28.160 1.00 29.00 BBBB ATOM 2750 CA PRO B 22 2.986 −39.252 −31.086 1.00 26.12 BBBB ATOM 2756 CA GLY B 23 0.787 −41.864 −32.752 1.00 25.07 BBBB ATOM 2760 CA LEU B 24 −2.201 −39.551 −32.401 1.00 25.32 BBBB ATOM 2768 CA ALA B 25 −0.197 −36.754 −34.013 1.00 25.94 BBBB ATOM 2773 CA VAL B 26 0.466 −38.955 −37.056 1.00 25.70 BBBB ATOM 2780 CA ALA B 27 −3.116 −40.222 −37.199 1.00 26.15 BBBB ATOM 2785 CA HIS B 28 −4.574 −36.702 −37.190 1.00 29.32 BBBB ATOM 2795 CA HIS B 29 −2.070 −35.623 −39.806 1.00 32.38 BBBB ATOM 2805 CA LEU B 30 −3.136 −38.417 −42.162 1.00 32.00 BBBB ATOM 2813 CA MET B 31 −6.849 −38.064 −41.424 1.00 34.91 BBBB ATOM 2821 CA ALA B 32 −6.510 −34.511 −42.722 1.00 37.55 BBBB ATOM 2826 CA GLN B 33 −5.182 −36.070 −45.938 1.00 38.24 BBBB ATOM 2835 CA GLY B 34 −8.305 −38.169 −46.353 1.00 35.75 BBBB ATOM 2839 CA TRP B 35 −7.016 −41.246 −44.508 1.00 34.58 BBBB ATOM 2853 CA GLN B 36 −9.175 −43.535 −42.402 1.00 35.40 BBBB ATOM 2862 CA VAL B 37 −7.417 −44.516 −39.184 1.00 34.16 BBBB ATOM 2869 CA ARG B 38 −8.219 −47.286 −36.730 1.00 31.56 BBBB ATOM 2880 CA TRP B 39 −6.456 −48.070 −33.471 1.00 27.41 BBBB ATOM 2894 CA LEU B 40 −5.200 −51.364 −32.026 1.00 24.71 BBBB ATOM 2902 CA GLY B 41 −4.691 −51.450 −28.257 1.00 23.47 BBBB ATOM 2906 CA THR B 42 −5.787 −53.141 −25.027 1.00 29.84 BBBB ATOM 2913 CA ALA B 43 −9.000 −52.595 −23.047 1.00 38.81 BBBB ATOM 2918 CA ASP B 44 −7.455 −51.942 −19.632 1.00 44.47 BBBB ATOM 2926 CA ARG B 45 −4.887 −49.367 −20.763 1.00 40.44 BBBB ATOM 2937 CA MET B 46 −4.881 −45.581 −21.249 1.00 36.33 BBBB ATOM 2945 CA GLU B 47 −5.458 −45.655 −25.029 1.00 31.79 BBBB ATOM 2954 CA ALA B 48 −8.821 −47.344 −24.414 1.00 32.58 BBBB ATOM 2959 CA ASP B 49 −10.143 −44.065 −23.009 1.00 35.60 BBBB ATOM 2967 CA LEU B 50 −8.026 −41.484 −24.840 1.00 33.49 BBBB ATOM 2975 CA VAL B 51 −8.299 −42.641 −28.449 1.00 32.68 BBBB ATOM 2983 CA PRO B 52 −12.111 −42.601 −28.453 1.00 34.43 BBBB ATOM 2989 CA LYS B 53 −11.998 −39.054 −27.064 1.00 36.73 BBBB ATOM 2998 CA HIS B 54 −10.116 −38.212 −30.259 1.00 34.62 BBBB ATOM 3008 CA GLY B 55 −12.938 −39.481 −32.447 1.00 35.34 BBBB ATOM 3012 CA ILE B 56 −10.909 −42.517 −33.514 1.00 33.81 BBBB ATOM 3020 CA GLU B 57 −12.228 −46.083 −33.467 1.00 34.16 BBBB ATOM 3029 CA ILE B 58 −10.217 −48.658 −31.553 1.00 31.38 BBBB ATOM 3037 CA ASP B 59 −10.039 −52.442 −31.720 1.00 31.09 BBBB ATOM 3045 CA PHE B 60 −8.809 −54.410 −28.713 1.00 30.32 BBBB ATOM 3056 CA ILE B 61 −6.832 −57.616 −28.269 1.00 28.55 BBBB ATOM 3064 CA ARG B 62 −5.709 −59.416 −25.133 1.00 30.76 BBBB ATOM 3075 CA ILE B 63 −2.036 −59.770 −24.231 1.00 31.38 BBBB ATOM 3083 CA SER B 64 −2.356 −60.520 −20.505 1.00 37.51 BBBB ATOM 3089 CA GLY B 65 0.679 −62.355 −19.199 1.00 37.13 BBBB ATOM 3093 CA LEU B 66 2.591 −61.413 −22.355 1.00 33.17 BBBB ATOM 3101 CA ARG B 67 3.671 −57.928 −21.277 1.00 30.90 BBBB ATOM 3112 CA GLY B 68 7.380 −57.427 −20.685 1.00 26.79 BBBB ATOM 3116 CA LYS B 69 8.238 −60.463 −22.796 1.00 23.93 BBBB ATOM 3125 CA GLY B 70 10.755 −60.229 −25.636 1.00 22.26 BBBB ATOM 3129 CA ILE B 71 10.357 −62.386 −28.762 1.00 23.55 BBBB ATOM 3137 CA LYS B 72 12.038 −65.491 −27.343 1.00 24.92 BBBB ATOM 3146 CA ALA B 73 9.839 −65.306 −24.233 1.00 21.18 BBBB ATOM 3151 CA LEU B 74 6.745 −64.762 −26.387 1.00 19.36 BBBB ATOM 3159 CA ILE B 75 7.434 −67.768 −28.601 1.00 21.18 BBBB ATOM 3167 CA ALA B 76 7.996 −69.726 −25.374 1.00 21.72 BBBB ATOM 3172 CA ALA B 77 4.289 −69.121 −24.655 1.00 21.07 BBBB ATOM 3178 CA PRO B 78 2.772 −70.846 −27.771 1.00 20.95 BBBB ATOM 3184 CA LEU B 79 −0.896 −70.728 −26.783 1.00 21.32 BBBB ATOM 3192 CA ARG B 80 −0.980 −67.115 −25.637 1.00 21.30 BBBB ATOM 3203 CA ILE B 81 1.113 −65.621 −28.421 1.00 19.47 BBBB ATOM 3211 CA PHE B 82 −0.875 −67.582 −31.038 1.00 19.15 BBBB ATOM 3222 CA ASN B 83 −4.150 −66.332 −29.577 1.00 20.90 BBBB ATOM 3230 CA ALA B 84 −3.177 −62.647 −29.484 1.00 19.30 BBBB ATOM 3235 CA TRP B 85 −1.820 −63.111 −33.032 1.00 20.56 BBBB ATOM 3249 CA ARG B 86 −5.140 −64.660 −34.166 1.00 23.28 BBBB ATOM 3260 CA GLN B 87 −7.101 −61.802 −32.567 1.00 24.07 BBBB ATOM 3269 CA ALA B 88 −4.996 −59.183 −34.355 1.00 23.78 BBBB ATOM 3274 CA ARG B 89 −5.285 −61.111 −37.636 1.00 24.94 BBBB ATOM 3285 CA ALA B 90 −9.088 −61.151 −37.383 1.00 26.16 BBBB ATOM 3290 CA ILE B 91 −9.108 −57.400 −36.733 1.00 26.97 BBBB ATOM 3298 CA MET B 92 −6.872 −56.693 −39.717 1.00 29.03 BBBB ATOM 3306 CA LYS B 93 −8.735 −59.038 −42.050 1.00 33.20 BBBB ATOM 3315 CA ALA B 94 −11.943 −57.157 −41.183 1.00 33.62 BBBB ATOM 3320 CA TYR B 95 −10.504 −53.620 −41.224 1.00 33.83 BBBB ATOM 3332 CA LYS B 96 −8.104 −54.327 −44.122 1.00 33.85 BBBB ATOM 3342 CA PRO B 97 −5.490 −51.623 −43.419 1.00 31.82 BBBB ATOM 3348 CA ASP B 98 −3.049 −50.685 −46.188 1.00 29.78 BBBB ATOM 3356 CA VAL B 99 −0.296 −50.214 −43.660 1.00 26.75 BBBB ATOM 3363 CA VAL B 100 0.227 −50.613 −39.936 1.00 23.59 BBBB ATOM 3370 CA LEU B 101 2.214 −48.199 −37.797 1.00 21.59 BBBB ATOM 3378 CA GLY B 102 3.796 −49.357 −34.549 1.00 19.23 BBBB ATOM 3382 CA MET B 103 4.892 −46.597 −32.191 1.00 18.93 BBBB ATOM 3389 N GLY B 104 5.640 −48.450 −30.827 1.00 21.56 BBBB ATOM 3390 CA GLY B 104 6.275 −49.080 −29.686 1.00 21.89 BBBB ATOM 3391 C GLY B 104 5.192 −49.614 −28.764 1.00 23.28 BBBB ATOM 3392 O GLY B 104 4.009 −49.353 −28.980 1.00 22.50 BBBB ATOM 3394 CA GLY B 105 4.593 −50.905 −26.827 1.00 23.54 BBBB ATOM 3398 CA TYR B 106 3.818 −54.554 −26.159 1.00 22.37 BBBB ATOM 3410 CA VAL B 107 0.557 −54.694 −28.099 1.00 18.06 BBBB ATOM 3417 CA SER B 108 2.488 −53.892 −31.290 1.00 19.67 BBBB ATOM 3423 CA GLY B 109 4.251 −57.256 −31.023 1.00 20.03 BBBB ATOM 3428 CA PRO B 110 1.251 −59.478 −31.855 1.00 18.99 BBBB ATOM 3434 CA GLY B 111 −0.160 −56.702 −34.025 1.00 19.60 BBBB ATOM 3438 CA GLY B 112 3.014 −56.417 −36.074 1.00 19.97 BBBB ATOM 3442 CA LEU B 113 3.265 −60.184 −36.429 1.00 19.49 BBBB ATOM 3450 CA ALA B 114 −0.334 −60.292 −37.661 1.00 18.70 BBBB ATOM 3455 CA ALA B 115 0.167 −57.516 −40.229 1.00 21.84 BBBB ATOM 3460 CA TRP B 116 3.365 −59.126 −41.478 1.00 23.22 BBBB ATOM 3474 CA SER B 117 1.735 −62.573 −41.873 1.00 22.61 BBBB ATOM 3480 CA LEU B 118 −1.069 −60.957 −43.882 1.00 25.70 BBBB ATOM 3488 CA GLY B 119 1.354 −59.174 −46.192 1.00 27.80 BBBB ATOM 3492 CA ILE B 120 0.568 −55.744 −44.731 1.00 24.85 BBBB ATOM 3501 CA PRO B 121 3.625 −53.477 −44.591 1.00 22.63 BBBB ATOM 3507 CA VAL B 122 4.743 −52.594 −41.083 1.00 22.03 BBBB ATOM 3514 CA VAL B 123 6.200 −49.184 −40.310 1.00 20.82 BBBB ATOM 3521 CA LEU B 124 7.749 −48.485 −36.915 1.00 22.10 BBBB ATOM 3528 N HIS B 125 8.182 −46.638 −35.447 1.00 21.40 BBBB ATOM 3529 CA HIS B 125 8.814 −45.413 −34.981 1.00 21.42 BBBB ATOM 3530 CB HIS B 125 7.858 −44.218 −35.067 1.00 21.57 BBBB ATOM 3531 CG HIS B 125 8.432 −42.948 −34.511 1.00 23.73 BBBB ATOM 3532 CD2 HIS B 125 8.300 −42.368 −33.295 1.00 22.15 BBBB ATOM 3533 ND1 HIS B 125 9.274 −42.127 −35.236 1.00 26.23 BBBB ATOM 3534 CE1 HIS B 125 9.631 −41.095 −34.490 1.00 24.20 BBBB ATOM 3535 NE2 HIS B 125 9.054 −41.218 −33.307 1.00 26.07 BBBB ATOM 3536 C HIS B 125 9.196 −45.642 −33.519 1.00 21.70 BBBB ATOM 3537 O HIS B 125 8.378 −46.117 −32.725 1.00 19.81 BBBB ATOM 3538 N GLU B 126 10.444 −45.332 −33.186 1.00 21.20 BBBB ATOM 3539 CA GLU B 126 10.947 −45.452 −31.817 1.00 22.15 BBBB ATOM 3540 CB GLU B 126 12.252 −46.246 −31.790 1.00 21.99 BBBB ATOM 3541 CG GLU B 126 12.958 −46.206 −30.439 1.00 22.04 BBBB ATOM 3542 CD GLU B 126 12.119 −46.824 −29.338 1.00 21.43 BBBB ATOM 3543 OE1 GLU B 126 11.767 −48.014 −29.471 1.00 21.92 BBBB ATOM 3544 OE2 GLU B 126 11.807 −46.124 −28.349 1.00 21.08 BBBB ATOM 3545 C GLU B 126 11.205 −44.027 −31.326 1.00 21.93 BBBB ATOM 3546 O GLU B 126 12.016 −43.300 −31.908 1.00 21.33 BBBB ATOM 3548 CA GLN B 127 10.682 −42.270 −29.735 1.00 22.81 BBBB ATOM 3557 CA ASN B 128 13.406 −43.097 −27.216 1.00 22.96 BBBB ATOM 3565 CA GLY B 129 17.203 −43.019 −27.294 1.00 25.36 BBBB ATOM 3569 CA ILE B 130 17.160 −46.716 −26.488 1.00 28.00 BBBB ATOM 3577 CA ALA B 131 14.978 −49.139 −28.461 1.00 25.88 BBBB ATOM 3582 CA GLY B 132 12.007 −50.532 −26.568 1.00 24.05 BBBB ATOM 3586 CA LEU B 133 11.903 −54.293 −26.020 1.00 24.54 BBBB ATOM 3594 CA THR B 134 9.202 −54.860 −28.639 1.00 21.22 BBBB ATOM 3601 CA ASN B 135 10.407 −52.419 −31.324 1.00 20.50 BBBB ATOM 3609 CA LYS B 136 13.886 −53.949 −31.144 1.00 22.79 BBBB ATOM 3618 CA TRP B 137 12.753 −57.345 −32.424 1.00 22.06 BBBB ATOM 3632 CA LEU B 138 9.744 −56.188 −34.431 1.00 23.15 BBBB ATOM 3640 CA ALA B 139 12.128 −54.092 −36.542 1.00 25.29 BBBB ATOM 3645 CA LYS B 140 13.279 −57.337 −38.182 1.00 28.05 BBBB ATOM 3654 CA ILE B 141 9.963 −57.818 −40.016 1.00 26.09 BBBB ATOM 3662 CA ALA B 142 9.331 −54.107 −40.498 1.00 25.03 BBBB ATOM 3667 CA THR B 143 9.262 −52.595 −43.984 1.00 26.10 BBBB ATOM 3674 CA LYS B 144 10.436 −49.238 −42.618 1.00 24.73 BBBB ATOM 3683 CA VAL B 145 11.947 −48.311 −39.252 1.00 23.62 BBBB ATOM 3690 CA MET B 146 12.338 −44.736 −37.993 1.00 23.15 BBBB ATOM 3698 CA GLN B 147 13.762 −43.418 −34.712 1.00 25.05 BBBB ATOM 3707 CA ALA B 148 13.559 −40.032 −33.009 1.00 26.88 BBBB ATOM 3712 CA PHE B 149 17.239 −39.820 −32.098 1.00 29.39 BBBB ATOM 3724 CA PRO B 150 20.310 −41.541 −33.535 1.00 31.87 BBBB ATOM 3730 CA GLY B 151 21.629 −44.537 −31.595 1.00 32.62 BBBB ATOM 3734 CA ALA B 152 18.447 −46.476 −30.753 1.00 32.71 BBBB ATOM 3739 CA PHE B 153 18.925 −48.506 −33.937 1.00 34.83 BBBB ATOM 3751 CA PRO B 154 22.158 −48.751 −35.993 1.00 38.97 BBBB ATOM 3757 CA ASN B 155 20.765 −47.568 −39.346 1.00 41.08 BBBB ATOM 3765 CA ALA B 156 17.170 −46.407 −38.843 1.00 37.55 BBBB ATOM 3770 CA GLU B 157 16.367 −43.044 −40.460 1.00 34.40 BBBB ATOM 3779 CA VAL B 158 16.337 −40.344 −37.764 1.00 31.16 BBBB ATOM 3786 CA VAL B 159 13.155 −38.265 −37.889 1.00 28.10 BBBB ATOM 3793 CA GLY B 160 12.724 −36.921 −34.355 1.00 26.93 BBBB ATOM 3797 CA ASN B 161 9.456 −36.807 −32.375 1.00 25.27 BBBB ATOM 3806 CA PRO B 162 6.315 −34.747 −33.004 1.00 26.14 BBBB ATOM 3812 CA VAL B 163 6.456 −31.379 −31.216 1.00 27.75 BBBB ATOM 3819 CA ARG B 164 3.667 −28.953 −30.246 1.00 32.36 BBBB ATOM 3830 CA THR B 165 3.038 −26.307 −32.924 1.00 31.74 BBBB ATOM 3837 CA ASP B 166 3.252 −23.404 −30.466 1.00 30.64 BBBB ATOM 3845 CA VAL B 167 6.746 −24.503 −29.440 1.00 25.91 BBBB ATOM 3852 CA LEU B 168 7.780 −25.002 −33.075 1.00 28.46 BBBB ATOM 3860 CA ALA B 169 6.580 −21.455 −33.756 1.00 31.43 BBBB ATOM 3865 CA LEU B 170 9.002 −19.905 −31.268 1.00 29.60 BBBB ATOM 3874 CA PRO B 171 11.611 −17.457 −32.642 1.00 30.11 BBBB ATOM 3880 CA LEU B 172 15.157 −18.780 −33.062 1.00 28.33 BBBB ATOM 3889 CA PRO B 173 17.450 −18.550 −29.977 1.00 25.25 BBBB ATOM 3895 CA GLN B 174 19.526 −15.527 −31.049 1.00 25.46 BBBB ATOM 3904 CA GLN B 175 16.365 −13.525 −31.718 1.00 28.47 BBBB ATOM 3913 CA ARG B 176 14.611 −14.635 −28.525 1.00 29.01 BBBB ATOM 3924 CA LEU B 177 17.673 −13.970 −26.331 1.00 29.90 BBBB ATOM 3932 CA ALA B 178 18.766 −10.776 −28.131 1.00 30.78 BBBB ATOM 3937 CA GLY B 179 19.846 −7.993 −25.784 1.00 30.10 BBBB ATOM 3941 CA ARG B 180 18.676 −9.965 −22.787 1.00 28.97 BBBB ATOM 3952 CA GLU B 181 20.545 −9.027 −19.621 1.00 31.79 BBBB ATOM 3961 CA GLY B 182 19.871 −9.586 −15.943 1.00 27.75 BBBB ATOM 3966 CA PRO B 183 19.450 −12.832 −13.913 1.00 22.93 BBBB ATOM 3972 CA VAL B 184 19.524 −16.146 −15.729 1.00 18.01 BBBB ATOM 3979 CA ARG B 185 15.873 −17.216 −16.011 1.00 17.62 BBBB ATOM 3990 CA VAL B 186 15.508 −20.771 −14.741 1.00 16.47 BBBB ATOM 3997 CA LEU B 187 12.361 −22.710 −15.604 1.00 16.75 BBBB ATOM 4005 CA VAL B 188 11.774 −25.775 −13.381 1.00 18.41 BBBB ATOM 4012 CA VAL B 189 9.298 −28.234 −14.948 1.00 22.11 BBBB ATOM 4018 N GLY B 190 8.111 −29.887 −13.615 1.00 25.60 BBBB ATOM 4019 CA GLY B 190 7.914 −31.188 −12.994 1.00 27.28 BBBB ATOM 4020 C GLY B 190 6.808 −32.026 −13.604 1.00 29.67 BBBB ATOM 4021 O GLY B 190 6.668 −33.208 −13.283 1.00 29.86 BBBB ATOM 4022 N GLY B 191 6.025 −31.430 −14.497 1.00 30.56 BBBB ATOM 4023 CA GLY B 191 4.935 −32.163 −15.115 1.00 31.94 BBBB ATOM 4024 C GLY B 191 3.676 −32.104 −14.269 1.00 33.11 BBBB ATOM 4025 O GLY B 191 3.691 −31.556 −13.165 1.00 32.14 BBBB ATOM 4026 N SER B 192 2.587 −32.673 −14.779 1.00 34.23 BBBB ATOM 4027 CA SER B 192 1.313 −32.665 −14.064 1.00 35.91 BBBB ATOM 4028 CB SER B 192 0.283 −33.532 −14.801 1.00 36.87 BBBB ATOM 4029 OG SER B 192 0.702 −34.887 −14.877 1.00 39.58 BBBB ATOM 4030 C SER B 192 1.419 −33.128 −12.609 1.00 36.41 BBBB ATOM 4031 O SER B 192 0.862 −32.499 −11.714 1.00 35.78 BBBB ATOM 4033 CA GLN B 193 2.292 −34.763 −11.033 1.00 38.53 BBBB ATOM 4041 N GLY B 194 4.291 −33.398 −10.986 1.00 36.47 BBBB ATOM 4042 CA GLY B 194 5.398 −32.711 −10.350 1.00 35.02 BBBB ATOM 4043 C GLY B 194 6.584 −33.630 −10.146 1.00 34.51 BBBB ATOM 4044 O GLY B 194 6.442 −34.851 −10.191 1.00 34.26 BBBB ATOM 4045 N ALA B 195 7.761 −33.045 −9.938 1.00 33.54 BBBB ATOM 4046 CA ALA B 195 8.977 −33.819 −9.709 1.00 33.12 BBBB ATOM 4047 CB ALA B 195 10.073 −33.387 −10.679 1.00 33.17 BBBB ATOM 4048 C ALA B 195 9.423 −33.590 −8.267 1.00 32.87 BBBB ATOM 4049 O ALA B 195 9.955 −32.533 −7.923 1.00 31.47 BBBB ATOM 4051 CA ARG B 196 9.538 −34.512 −6.010 1.00 32.63 BBBB ATOM 4062 CA ILE B 197 13.329 −34.168 −6.164 1.00 28.10 BBBB ATOM 4070 CA LEU B 198 13.069 −30.833 −8.003 1.00 26.58 BBBB ATOM 4078 CA ASN B 199 10.497 −29.447 −5.563 1.00 27.07 BBBB ATOM 4086 CA GLN B 200 12.955 −30.326 −2.794 1.00 30.10 BBBB ATOM 4095 CA THR B 201 16.215 −29.345 −4.474 1.00 27.34 BBBB ATOM 4102 CA MET B 202 15.567 −26.048 −6.268 1.00 23.68 BBBB ATOM 4111 CA PRO B 203 14.608 −23.963 −3.220 1.00 23.84 BBBB ATOM 4117 CA GLN B 204 18.033 −24.708 −1.684 1.00 26.34 BBBB ATOM 4126 CA VAL B 205 19.672 −24.033 −5.043 1.00 24.44 BBBB ATOM 4133 CA ALA B 206 17.980 −20.610 −5.013 1.00 22.84 BBBB ATOM 4138 CA ALA B 207 19.442 −19.857 −1.576 1.00 26.65 BBBB ATOM 4143 CA LYS B 208 22.915 −20.595 −2.919 1.00 28.31 BBBB ATOM 4152 CA LEU B 209 22.577 −18.640 −6.171 1.00 25.68 BBBB ATOM 4160 CA GLY B 210 20.675 −15.628 −4.804 1.00 26.56 BBBB ATOM 4164 CA ASP B 211 20.370 −12.647 −7.190 1.00 28.28 BBBB ATOM 4172 CA SER B 212 22.098 −14.474 −10.067 1.00 25.73 BBBB ATOM 4178 CA VAL B 213 18.925 −16.308 −11.116 1.00 20.76 BBBB ATOM 4185 CA THR B 214 15.204 −15.726 −11.337 1.00 19.60 BBBB ATOM 4192 CA ILE B 215 13.076 −18.850 −11.169 1.00 18.75 BBBB ATOM 4200 CA TRP B 216 9.661 −19.973 −12.378 1.00 19.34 BBBB ATOM 4214 CA HIS B 217 9.015 −23.303 −10.680 1.00 21.06 BBBB ATOM 4224 CA GLN B 218 6.149 −25.594 −11.735 1.00 24.30 BBBB ATOM 4233 CA SER B 219 5.463 −27.800 −8.684 1.00 26.73 BBBB ATOM 4239 CA GLY B 220 2.855 −30.242 −9.961 1.00 30.53 BBBB ATOM 4243 CA LYS B 221 −0.657 −30.914 −8.628 1.00 35.12 BBBB ATOM 4252 CA GLY B 222 −1.195 −29.899 −5.011 1.00 35.34 BBBB ATOM 4256 CA SER B 223 2.451 −28.934 −4.418 1.00 33.98 BBBB ATOM 4262 CA GLN B 224 2.187 −25.208 −5.186 1.00 33.71 BBBB ATOM 4271 CA GLN B 225 1.823 −24.239 −1.519 1.00 32.32 BBBB ATOM 4280 CA SER B 226 4.701 −26.309 −0.122 1.00 28.30 BBBB ATOM 4286 CA VAL B 227 7.214 −25.247 −2.791 1.00 24.28 BBBB ATOM 4293 CA GLU B 228 6.178 −21.592 −2.387 1.00 27.23 BBBB ATOM 4302 CA GLN B 229 6.853 −22.046 1.329 1.00 28.38 BBBB ATOM 4311 CA ALA B 230 10.185 −23.754 0.682 1.00 26.18 BBBB ATOM 4316 CA TYR B 231 11.371 −20.766 −1.366 1.00 25.47 BBBB ATOM 4328 CA ALA B 232 10.342 −18.322 1.368 1.00 27.51 BBBB ATOM 4333 CA GLU B 233 12.145 −20.441 3.966 1.00 30.87 BBBB ATOM 4342 CA ALA B 234 15.215 −20.417 1.714 1.00 28.48 BBBB ATOM 4347 CA GLY B 235 15.033 −16.627 1.815 1.00 26.23 BBBB ATOM 4351 CA GLN B 236 14.121 −16.198 −1.870 1.00 25.53 BBBB ATOM 4361 CA PRO B 237 10.336 −15.587 −1.720 1.00 24.65 BBBB ATOM 4367 CA GLN B 238 10.277 −13.558 −4.945 1.00 24.29 BBBB ATOM 4376 CA HIS B 239 10.526 −16.608 −7.201 1.00 22.08 BBBB ATOM 4386 CA LYS B 240 7.375 −17.589 −9.105 1.00 23.26 BBBB ATOM 4395 CA VAL B 241 5.740 −20.911 −8.277 1.00 23.78 BBBB ATOM 4402 CA THR B 242 2.758 −22.301 −10.177 1.00 25.93 BBBB ATOM 4409 CA GLU B 243 0.999 −25.651 −9.837 1.00 27.03 BBBB ATOM 4418 CA PHE B 244 0.964 −26.068 −13.620 1.00 26.54 BBBB ATOM 4429 CA ILE B 245 1.932 −24.242 −16.802 1.00 28.48 BBBB ATOM 4437 CA ASP B 246 −0.754 −24.396 −19.457 1.00 36.00 BBBB ATOM 4445 CA ASP B 247 1.245 −22.392 −21.999 1.00 30.74 BBBB ATOM 4453 CA MET B 248 4.625 −24.136 −22.138 1.00 28.41 BBBB ATOM 4461 CA ALA B 249 5.512 −22.216 −25.290 1.00 24.67 BBBB ATOM 4466 CA ALA B 250 5.188 −18.933 −23.390 1.00 21.78 BBBB ATOM 4471 CA ALA B 251 7.301 −20.259 −20.501 1.00 20.85 BBBB ATOM 4476 CA TYR B 252 9.972 −21.616 −22.886 1.00 22.78 BBBB ATOM 4488 CA ALA B 253 10.131 −18.224 −24.636 1.00 23.54 BBBB ATOM 4493 CA TRP B 254 10.829 −16.534 −21.303 1.00 19.76 BBBB ATOM 4507 CA ALA B 255 13.399 −19.025 −20.003 1.00 19.51 BBBB ATOM 4512 CA ASP B 256 17.176 −19.026 −20.434 1.00 17.58 BBBB ATOM 4520 CA VAL B 257 17.535 −22.603 −19.194 1.00 18.53 BBBB ATOM 4527 CA VAL B 258 15.208 −25.456 −18.234 1.00 19.32 BBBB ATOM 4534 CA VAL B 259 15.581 −27.957 −15.374 1.00 19.85 BBBB ATOM 4541 CA CYS B 260 13.454 −31.055 −15.946 1.00 22.00 BBBB ATOM 4546 N ARG B 261 12.937 −33.397 −16.212 1.00 22.34 BBBB ATOM 4547 CA ARG B 261 13.170 −34.800 −16.515 1.00 23.75 BBBB ATOM 4548 CB ARG B 261 11.964 −35.663 −16.104 1.00 27.16 BBBB ATOM 4549 CG ARG B 261 11.376 −35.337 −14.738 1.00 31.82 BBBB ATOM 4550 CD ARG B 261 11.490 −36.473 −13.732 1.00 36.33 BBBB ATOM 4551 NE ARG B 261 12.865 −36.721 −13.323 1.00 38.48 BBBB ATOM 4552 CZ ARG B 261 13.218 −37.176 −12.125 1.00 37.25 BBBB ATOM 4553 NH1 ARG B 261 12.295 −37.433 −11.204 1.00 38.46 BBBB ATOM 4554 NH2 ARG B 261 14.499 −37.370 −11.848 1.00 36.79 BBBB ATOM 4555 C ARG B 261 13.351 −34.871 −18.032 1.00 23.98 BBBB ATOM 4556 O ARG B 261 13.117 −33.883 −18.746 1.00 22.44 BBBB ATOM 4558 CA SER B 262 13.975 −36.189 −19.948 1.00 23.18 BBBB ATOM 4563 N GLY B 263 11.850 −37.151 −20.619 1.00 22.74 BBBB ATOM 4564 CA GLY B 263 11.026 −38.079 −21.361 1.00 22.85 BBBB ATOM 4565 C GLY B 263 11.392 −37.793 −22.813 1.00 24.06 BBBB ATOM 4566 O GLY B 263 11.908 −36.705 −23.121 1.00 22.75 BBBB ATOM 4567 N ALA B 264 11.130 −38.739 −23.708 1.00 23.37 BBBB ATOM 4568 CA ALA B 264 11.482 −38.564 −25.115 1.00 24.25 BBBB ATOM 4569 CB ALA B 264 11.133 −39.829 −25.894 1.00 24.58 BBBB ATOM 4570 C ALA B 264 10.843 −37.343 −25.783 1.00 24.29 BBBB ATOM 4571 O ALA B 264 11.523 −36.572 −26.470 1.00 24.33 BBBB ATOM 4573 CA LEU B 265 8.846 −36.037 −26.205 1.00 24.66 BBBB ATOM 4581 CA THR B 266 10.194 −33.557 −23.657 1.00 22.34 BBBB ATOM 4588 CA VAL B 267 13.730 −33.762 −25.023 1.00 21.11 BBBB ATOM 4595 CA SER B 268 12.411 −33.191 −28.567 1.00 21.96 BBBB ATOM 4600 N GLU B 269 10.928 −31.563 −27.557 1.00 21.64 BBBB ATOM 4601 CA GLU B 269 10.282 −30.272 −27.378 1.00 21.95 BBBB ATOM 4602 CB GLU B 269 9.213 −30.399 −26.292 1.00 24.72 BBBB ATOM 4603 CG GLU B 269 8.480 −29.128 −25.940 1.00 27.67 BBBB ATOM 4604 CD GLU B 269 7.385 −29.380 −24.908 1.00 30.05 BBBB ATOM 4605 OE1 GLU B 269 6.325 −29.915 −25.287 1.00 31.50 BBBB ATOM 4606 OE2 GLU B 269 7.591 −29.057 −23.719 1.00 29.84 BBBB ATOM 4607 C GLU B 269 11.321 −29.214 −26.999 1.00 21.68 BBBB ATOM 4608 O GLU B 269 11.301 −28.095 −27.518 1.00 18.12 BBBB ATOM 4610 CA ILE B 270 13.295 −28.698 −25.638 1.00 20.62 BBBB ATOM 4618 CA ALA B 271 15.440 −29.058 −28.776 1.00 22.45 BBBB ATOM 4623 CA ALA B 272 12.719 −27.451 −30.898 1.00 22.17 BBBB ATOM 4628 CA ALA B 273 12.361 −24.596 −28.407 1.00 21.97 BBBB ATOM 4633 CA GLY B 274 16.093 −24.023 −28.709 1.00 21.07 BBBB ATOM 4637 CA LEU B 275 16.666 −24.057 −24.966 1.00 19.78 BBBB ATOM 4646 CA PRO B 276 19.651 −25.199 −22.875 1.00 16.62 BBBB ATOM 4652 CA ALA B 277 18.638 −27.807 −20.321 1.00 15.80 BBBB ATOM 4657 CA LEU B 278 19.896 −29.429 −17.145 1.00 18.48 BBBB ATOM 4665 CA PHE B 279 18.266 −32.838 −17.392 1.00 21.59 BBBB ATOM 4676 CA VAL B 280 17.502 −34.902 −14.281 1.00 25.67 BBBB ATOM 4682 N PRO B 281 17.324 −37.080 −15.370 1.00 27.08 BBBB ATOM 4683 CD PRO B 281 18.750 −37.057 −15.726 1.00 27.31 BBBB ATOM 4684 CA PRO B 281 16.698 −38.320 −15.824 1.00 29.05 BBBB ATOM 4685 CB PRO B 281 17.851 −39.071 −16.492 1.00 29.44 BBBB ATOM 4686 CG PRO B 281 18.791 −37.992 −16.895 1.00 29.67 BBBB ATOM 4687 C PRO B 281 16.092 −39.121 −14.684 1.00 31.51 BBBB ATOM 4688 O PRO B 281 16.675 −39.223 −13.603 1.00 32.26 BBBB ATOM 4690 CA PHE B 282 14.246 −40.496 −13.926 1.00 37.13 BBBB ATOM 4701 CA GLN B 283 16.319 −43.395 −12.591 1.00 41.11 BBBB ATOM 4710 CA HIS B 284 15.641 −46.917 −13.843 1.00 43.69 BBBB ATOM 4720 CA LYS B 285 17.767 −49.993 −14.571 1.00 45.34 BBBB ATOM 4729 CA ASP B 286 16.949 −49.299 −18.222 1.00 43.26 BBBB ATOM 4737 CA ARG B 287 17.951 −45.623 −17.883 1.00 36.28 BBBB ATOM 4748 CA GLN B 288 15.622 −44.804 −20.755 1.00 30.77 BBBB ATOM 4756 N GLN B 289 15.378 −42.554 −19.857 1.00 29.38 BBBB ATOM 4757 CA GLN B 289 15.474 −41.099 −19.904 1.00 29.46 BBBB ATOM 4758 CB GLN B 289 14.772 −40.472 −18.700 1.00 29.25 BBBB ATOM 4759 CG GLN B 289 13.265 −40.416 −18.883 1.00 29.32 BBBB ATOM 4760 CD GLN B 289 12.575 −39.585 −17.826 1.00 29.84 BBBB ATOM 4761 OE1 GLN B 289 13.191 −38.728 −17.188 1.00 29.52 BBBB ATOM 4762 NE2 GLN B 289 11.281 −39.821 −17.647 1.00 28.95 BBBB ATOM 4763 C GLN B 289 16.906 −40.613 −20.005 1.00 29.36 BBBB ATOM 4764 O GLN B 289 17.173 −39.557 −20.585 1.00 29.12 BBBB ATOM 4766 CA TYR B 290 19.228 −40.984 −19.550 1.00 29.55 BBBB ATOM 4778 CA TRP B 291 19.542 −42.282 −23.116 1.00 28.07 BBBB ATOM 4791 N ASN B 292 17.658 −40.779 −23.508 1.00 25.52 BBBB ATOM 4792 CA ASN B 292 16.902 −39.784 −24.270 1.00 26.06 BBBB ATOM 4793 CB ASN B 292 15.484 −39.599 −23.709 1.00 24.78 BBBB ATOM 4794 CG ASN B 292 14.590 −40.811 −23.928 1.00 24.46 BBBB ATOM 4795 OD1 ASN B 292 14.842 −41.641 −24.798 1.00 25.33 BBBB ATOM 4796 ND2 ASN B 292 13.523 −40.900 −23.146 1.00 23.83 BBBB ATOM 4797 C ASN B 292 17.605 −38.427 −24.258 1.00 25.99 BBBB ATOM 4798 O ASN B 292 17.566 −37.687 −25.244 1.00 26.18 BBBB ATOM 4799 N ALA B 293 18.242 −38.105 −23.139 1.00 25.66 BBBB ATOM 4800 CA ALA B 293 18.926 −36.822 −22.979 1.00 25.69 BBBB ATOM 4801 CB ALA B 293 18.940 −36.422 −21.506 1.00 24.17 BBBB ATOM 4802 C ALA B 293 20.346 −36.800 −23.521 1.00 25.67 BBBB ATOM 4803 O ALA B 293 20.855 −35.743 −23.902 1.00 25.52 BBBB ATOM 4805 CA LEU B 294 22.354 −38.088 −24.032 1.00 25.90 BBBB ATOM 4814 CA PRO B 295 21.998 −36.870 −27.635 1.00 26.15 BBBB ATOM 4820 CA LEU B 296 21.521 −33.265 −26.481 1.00 25.42 BBBB ATOM 4828 CA GLU B 297 24.354 −33.530 −23.953 1.00 28.78 BBBB ATOM 4837 CA LYS B 298 26.644 −34.947 −26.648 1.00 31.90 BBBB ATOM 4846 CA ALA B 299 25.773 −31.965 −28.847 1.00 30.38 BBBB ATOM 4851 CA GLY B 300 26.777 −29.635 −26.017 1.00 26.18 BBBB ATOM 4855 CA ALA B 301 23.214 −28.333 −25.638 1.00 22.50 BBBB ATOM 4860 CA ALA B 302 22.516 −29.770 −22.186 1.00 21.78 BBBB ATOM 4865 CA LYS B 303 23.979 −31.340 −19.048 1.00 25.86 BBBB ATOM 4874 CA ILE B 304 22.753 −34.598 −17.550 1.00 27.17 BBBB ATOM 4882 CA ILE B 305 22.843 −35.178 −13.813 1.00 29.01 BBBB ATOM 4890 CA GLU B 306 21.664 −38.702 −13.061 1.00 34.65 BBBB ATOM 4899 CA GLN B 307 20.377 −39.599 −9.613 1.00 40.54 BBBB ATOM 4909 CA PRO B 308 23.828 −40.891 −8.484 1.00 43.20 BBBB ATOM 4915 CA GLN B 309 25.247 −37.361 −8.787 1.00 43.46 BBBB ATOM 4924 CA LEU B 310 22.232 −35.166 −8.022 1.00 39.65 BBBB ATOM 4932 CA SER B 311 22.660 −32.714 −5.154 1.00 34.90 BBBB ATOM 4938 CA VAL B 312 21.990 −29.074 −4.341 1.00 31.50 BBBB ATOM 4945 CA ASP B 313 25.642 −28.202 −4.957 1.00 29.61 BBBB ATOM 4953 CA ALA B 314 25.782 −30.099 −8.254 1.00 26.47 BBBB ATOM 4958 CA VAL B 315 22.755 −28.215 −9.612 1.00 25.33 BBBB ATOM 4965 CA ALA B 316 23.888 −24.872 −8.199 1.00 27.13 BBBB ATOM 4970 CA ASN B 317 27.444 −25.246 −9.518 1.00 28.52 BBBB ATOM 4978 CA TBR B 318 26.174 −26.371 −12.906 1.00 27.04 BBBB ATOM 4985 CA LEU B 319 23.883 −23.370 −13.357 1.00 25.21 BBBB ATOM 4993 CA ALA B 320 26.445 −20.931 −11.957 1.00 24.59 BBBB ATOM 4998 CA GLY B 321 28.934 −22.031 −14.591 1.00 24.34 BBBB ATOM 5002 CA TRP B 322 26.738 −21.007 −17.521 1.00 21.72 BBBB ATOM 5016 CA SER B 323 27.141 −17.404 −18.692 1.00 19.04 BBBB ATOM 5022 CA ARG B 324 24.725 −15.741 −21.112 1.00 18.09 BBBB ATOM 5033 CA GLU B 325 27.220 −16.368 −23.954 1.00 16.96 BBBB ATOM 5042 CA THR B 326 27.460 −20.055 −23.070 1.00 16.39 BBBB ATOM 5049 CA LEU B 327 23.659 −20.305 −22.780 1.00 17.27 BBBB ATOM 5057 CA LEU B 328 23.175 −18.745 −26.222 1.00 17.39 BBBB ATOM 5065 CA THR B 329 25.567 −21.335 −27.688 1.00 21.30 BBBB ATOM 5072 CA MET B 330 23.771 −24.153 −25.870 1.00 19.91 BBBB ATOM 5080 CA ALA B 331 20.412 −22.871 −27.098 1.00 18.49 BBBB ATOM 5085 CA GLU B 332 21.626 −22.827 −30.704 1.00 21.47 BBBB ATOM 5094 CA ARG B 333 23.040 −26.330 −30.408 1.00 23.77 BBBB ATOM 5105 CA ALA B 334 19.648 −27.420 −29.063 1.00 22.88 BBBB ATOM 5110 CA ARG B 335 17.795 −25.892 −32.002 1.00 23.54 BBBB ATOM 5121 CA ALA B 336 20.330 −27.477 −34.372 1.00 26.85 BBBB ATOM 5126 CA ALA B 337 19.740 −30.925 −32.865 1.00 30.89 BBBB ATOM 5131 CA SER B 338 16.008 −30.432 −33.408 1.00 32.41 BBBB ATOM 5137 CA ILE B 339 13.882 −31.941 −36.187 1.00 34.35 BBBB ATOM 5146 CA PRO B 340 10.733 −29.730 −36.600 1.00 34.94 BBBB ATOM 5152 CA ASP B 341 8.711 −31.820 −39.056 1.00 33.33 BBBB ATOM 5160 CA ALA B 342 8.875 −35.238 −37.411 1.00 29.09 BBBB ATOM 5165 CA THR B 343 5.115 −35.696 −37.744 1.00 28.55 BBBB ATOM 5172 CA GLU B 344 5.085 −34.933 −41.480 1.00 32.00 BBBB ATOM 5181 CA ARG B 345 8.138 −37.123 −42.067 1.00 31.44 BBBB ATOM 5192 CA VAL B 346 6.578 −40.151 −40.384 1.00 28.61 BBBB ATOM 5199 CA ALA B 347 3.249 −39.617 −42.137 1.00 28.96 BBBB ATOM 5204 CA ASN B 348 5.035 −39.286 −45.493 1.00 34.56 BBBB ATOM 5212 CA GLU B 349 6.954 −42.540 −44.956 1.00 34.86 BBBB ATOM 5221 CA VAL B 350 3.767 −44.306 −43.919 1.00 33.79 BBBB ATOM 5228 CA SER B 351 2.196 −42.946 −47.095 1.00 36.67 BBBB ATOM 5234 CA ARG B 352 5.114 −44.088 −49.251 1.00 40.03 BBBB ATOM 5245 CA VAL B 353 5.089 −47.587 −47.737 1.00 42.78 BBBB ATOM 5252 CA ALA B 354 1.336 −47.957 −48.212 1.00 47.24 BBBB ATOM 5257 CA ARG B 355 2.035 −46.964 −51.824 1.00 52.71 BBBB ATOM 5268 CA ALA B 356 4.453 −49.913 −51.809 1.00 54.93 BBBB ATOM 5273 CA LEU B 357 7.023 −47.522 −53.289 1.00 57.81 BBBB END

TABLE 4 ATOMIC COORDINATES OF THE DONOR NUCLEOTIDE BINDING SITE REMARK 4 1MUR COMPLIES WITH FORMAT V. 2.0, MAY 11, 2000 ATOM 1 N LEU B 187 13.695 −22.128 −15.588 1.00 15.92 N ATOM 2 CA LEU B 187 12.361 −22.710 −15.604 1.00 16.75 C ATOM 3 C LEU B 187 12.450 −24.146 −15.085 1.00 16.85 C ATOM 4 O LEU B 187 13.115 −24.982 −15.688 1.00 17.18 O ATOM 5 CB LEU B 187 11.813 −22.701 −17.035 1.00 16.85 C ATOM 6 CG LEU B 187 10.445 −23.340 −17.276 1.00 18.63 C ATOM 7 CD1 LEU B 187 9.368 −22.478 −16.625 1.00 19.42 C ATOM 8 CD2 LEU B 187 10.198 −23.449 −18.783 1.00 19.11 C ATOM 9 N VAL B 188 11.788 −24.426 −13.964 1.00 18.20 N ATOM 10 CA VAL B 188 11.774 −25.775 −13.381 1.00 18.41 C ATOM 11 C VAL B 188 10.434 −26.440 −13.739 1.00 19.88 C ATOM 12 O VAL B 188 9.371 −25.967 −13.336 1.00 20.39 O ATOM 13 CB VAL B 188 11.902 −25.714 −11.842 1.00 18.98 C ATOM 14 CG1 VAL B 188 12.088 −27.126 −11.270 1.00 18.50 C ATOM 15 CG2 VAL B 188 13.061 −24.818 −11.449 1.00 18.83 C ATOM 16 N VAL B 189 10.493 −27.532 −14.496 1.00 21.55 N ATOM 17 CA VAL B 189 9.298 −28.234 −14.948 1.00 22.11 C ATOM 18 C VAL B 189 9.191 −29.639 −14.351 1.00 23.90 C ATOM 19 O VAL B 189 10.067 −30.478 −14.559 1.00 23.61 O ATOM 20 CB VAL B 189 9.299 −28.342 −16.488 1.00 22.50 C ATOM 21 CG1 VAL B 189 8.009 −29.013 −16.981 1.00 22.70 C ATOM 22 CG2 VAL B 189 9.470 −26.943 −17.101 1.00 21.26 C ATOM 23 N GLY B 190 8.111 −29.887 −13.615 1.00 25.60 N ATOM 24 CA GLY B 190 7.914 −31.188 −12.994 1.00 27.28 C ATOM 25 C GLY B 190 6.808 −32.026 −13.604 1.00 29.67 C ATOM 26 O GLY B 190 6.668 −33.208 −13.283 1.00 29.86 O ATOM 27 N GLY B 191 6.025 −31.430 −14.497 1.00 30.56 N ATOM 28 CA GLY B 191 4.935 −32.163 −15.115 1.00 31.94 C ATOM 29 C GLY B 191 3.676 −32.104 −14.269 1.00 33.11 C ATOM 30 O GLY B 191 3.691 −31.556 −13.165 1.00 32.14 O ATOM 31 N ALA B 195 7.761 −33.045 −9.938 1.00 33.54 N ATOM 32 CA ALA B 195 8.977 −33.819 −9.709 1.00 33.12 C ATOM 33 C ALA B 195 9.423 −33.590 −8.267 1.00 32.87 C ATOM 34 O ALA B 195 9.955 −32.533 −7.923 1.00 31.47 O ATOM 35 CB ALA B 195 10.073 −33.387 −10.679 1.00 33.17 C ATOM 36 N LEU B 198 12.897 −32.223 −7.590 1.00 27.07 N ATOM 37 CA LEU B 198 13.069 −30.833 −8.003 1.00 26.58 C ATOM 38 C LEU B 198 12.388 −29.893 −7.006 1.00 26.41 C ATOM 39 O LEU B 198 12.930 −28.835 −6.667 1.00 26.35 O ATOM 40 CB LEU B 198 12.504 −30.616 −9.412 1.00 25.88 C ATOM 41 CG LEU B 198 13.196 −31.408 −10.524 1.00 25.40 C ATOM 42 CD1 LEU B 198 12.625 −31.007 −11.874 1.00 26.54 C ATOM 43 CD2 LEU B 198 14.692 −31.146 −10.493 1.00 25.94 C ATOM 44 N TYR B 252 8.723 −21.314 −22.184 1.00 21.27 N ATOM 45 CA TYR B 252 9.972 −21.616 −22.886 1.00 22.78 C ATOM 46 C TYR B 252 10.566 −20.354 −23.516 1.00 23.57 C ATOM 47 O TYR B 252 11.784 −20.180 −23.550 1.00 23.91 O ATOM 48 CB TYR B 252 9.726 −22.661 −23.980 1.00 21.62 C ATOM 49 CG TYR B 252 9.662 −24.100 −23.505 1.00 23.34 C ATOM 50 CD1 TYR B 252 9.003 −25.065 −24.261 1.00 22.88 C ATOM 51 CD2 TYR B 252 10.288 −24.505 −22.319 1.00 22.30 C ATOM 52 CE1 TYR B 252 8.961 −26.392 −23.861 1.00 24.81 C ATOM 53 CE2 TYR B 252 10.253 −25.838 −21.912 1.00 23.56 C ATOM 54 CZ TYR B 252 9.590 −26.772 −22.687 1.00 24.26 C ATOM 55 OH TYR B 252 9.554 −28.088 −22.305 1.00 25.57 O ATOM 56 N VAL B 258 16.263 −24.643 −18.818 1.00 18.74 N ATOM 57 CA VAL B 258 15.208 −25.456 −18.234 1.00 19.32 C ATOM 58 C VAL B 258 15.799 −26.585 −17.389 1.00 19.70 C ATOM 59 O VAL B 258 16.808 −27.175 −17.758 1.00 18.96 O ATOM 60 CB VAL B 258 14.328 −26.100 −19.337 1.00 19.89 C ATOM 61 CG1 VAL B 258 13.101 −26.754 −18.714 1.00 19.81 C ATOM 62 CG2 VAL B 258 13.907 −25.041 −20.364 1.00 21.59 C ATOM 63 N VAL B 259 15.167 −26.861 −16.253 1.00 20.24 N ATOM 64 CA VAL B 259 15.581 −27.957 −15.374 1.00 19.85 C ATOM 65 C VAL B 259 14.382 −28.890 −15.371 1.00 20.02 C ATOM 66 O VAL B 259 13.301 −28.500 −14.942 1.00 21.88 O ATOM 67 CB VAL B 259 15.850 −27.483 −13.936 1.00 20.08 C ATOM 68 CG1 VAL B 259 16.222 −28.689 −13.059 1.00 20.22 C ATOM 69 CG2 VAL B 259 16.966 −26.453 −13.930 1.00 17.86 C ATOM 70 N CYS B 260 14.562 −30.111 −15.867 1.00 21.70 N ATOM 71 CA CYS B 260 13.454 −31.055 −15.946 1.00 22.00 C ATOM 72 C CYS B 260 13.903 −32.478 −16.242 1.00 21.86 C ATOM 73 O CYS B 260 15.087 −32.730 −16.496 1.00 21.34 O ATOM 74 CB CYS B 260 12.494 −30.618 −17.057 1.00 22.77 C ATOM 75 SG CYS B 260 13.297 −30.506 −18.711 1.00 22.15 S ATOM 76 N ARG B 261 12.937 −33.397 −16.212 1.00 22.34 N ATOM 77 CA ARG B 261 13.170 −34.800 −16.515 1.00 23.75 C ATOM 78 C ARG B 261 13.351 −34.871 −18.032 1.00 23.98 C ATOM 79 O ARG B 261 13.117 −33.883 −18.746 1.00 22.44 O ATOM 80 CB ARG B 261 11.964 −35.663 −16.104 1.00 27.16 C ATOM 81 CG ARG B 261 11.376 −35.337 −14.738 1.00 31.82 C ATOM 82 CD ARG B 261 11.490 −36.473 −13.732 1.00 36.33 C ATOM 83 NE ARG B 261 12.865 −36.721 −13.323 1.00 38.48 N ATOM 84 CZ ARG B 261 13.218 −37.176 −12.125 1.00 37.25 C ATOM 85 NH1 ARG B 261 12.295 −37.433 −11.204 1.00 38.46 N ATOM 86 NH2 ARG B 261 14.499 −37.370 −11.848 1.00 36.79 N ATOM 87 N SER B 262 13.740 −36.038 −18.527 1.00 22.00 N ATOM 88 CA SER B 262 13.975 −36.189 −19.948 1.00 23.18 C ATOM 89 C SER B 262 13.173 −37.263 −20.676 1.00 22.90 C ATOM 90 O SER B 262 13.738 −38.179 −21.274 1.00 23.25 O ATOM 91 CB SER B 262 15.481 −36.377 −20.203 1.00 24.45 C ATOM 92 OG SER B 262 16.043 −37.326 −19.311 1.00 25.79 O ATOM 93 N GLY B 263 11.850 −37.151 −20.619 1.00 22.74 N ATOM 94 CA GLY B 263 11.026 −38.079 −21.361 1.00 22.85 C ATOM 95 C GLY B 263 11.392 −37.793 −22.813 1.00 24.06 C ATOM 96 O GLY B 263 11.908 −36.705 −23.121 1.00 22.75 O ATOM 97 N ALA B 264 11.130 −38.739 −23.708 1.00 23.37 N ATOM 98 CA ALA B 264 11.482 −38.564 −25.115 1.00 24.25 C ATOM 99 C ALA B 264 10.843 −37.343 −25.783 1.00 24.29 C ATOM 100 O ALA B 264 11.523 −36.572 −26.470 1.00 24.33 O ATOM 101 CB ALA B 264 11.133 −39.829 −25.894 1.00 24.58 C ATOM 102 N LEU B 265 9.541 −37.167 −25.596 1.00 24.44 N ATOM 103 CA LEU B 265 8.846 −36.037 −26.205 1.00 24.66 C ATOM 104 C LEU B 265 9.331 −34.717 −25.613 1.00 24.47 C ATOM 105 O LEU B 265 9.374 −33.693 −26.301 1.00 23.85 O ATOM 106 CB LEU B 265 7.332 −36.183 −26.011 1.00 25.33 C ATOM 107 CG LEU B 265 6.760 −37.544 −26.426 1.00 27.97 C ATOM 108 CD1 LEU B 265 5.242 −37.541 −26.258 1.00 28.21 C ATOM 109 CD2 LEU B 265 7.146 −37.856 −27.878 1.00 27.40 C ATOM 110 N THR B 266 9.702 −34.747 −24.338 1.00 22.12 N ATOM 111 CA THR B 266 10.194 −33.557 −23.657 1.00 22.34 C ATOM 112 C THR B 266 11.535 −33.117 −24.226 1.00 21.15 C ATOM 113 O THR B 266 11.761 −31.926 −24.442 1.00 20.35 O ATOM 114 CB THR B 266 10.348 −33.803 −22.140 1.00 22.35 C ATOM 115 CG1 THR B 266 9.061 −34.087 −21.583 1.00 24.46 O ATOM 116 CG2 THR B 266 10.945 −32.573 −21.444 1.00 24.00 C ATOM 117 N VAL B 267 12.427 −34.075 −24.461 1.00 20.46 N ATOM 118 CA VAL B 267 13.730 −33.762 −25.023 1.00 21.11 C ATOM 119 C VAL B 267 13.548 −33.138 −26.416 1.00 21.34 C ATOM 120 O VAL B 267 14.188 −32.135 −26.747 1.00 19.99 O ATOM 121 CB VAL B 267 14.614 −35.039 −25.114 1.00 21.54 C ATOM 122 CG1 VAL B 267 15.903 −34.740 −25.865 1.00 20.72 C ATOM 123 CG2 VAL B 267 14.938 −35.541 −23.708 1.00 20.45 C ATOM 124 N SER B 268 12.663 −33.717 −27.222 1.00 21.61 N ATOM 125 CA SER B 268 12.411 −33.191 −28.567 1.00 21.96 C ATOM 126 C SER B 268 11.817 −31.790 −28.519 1.00 21.81 C ATOM 127 O SER B 268 12.158 −30.933 −29.336 1.00 22.60 O ATOM 128 CB SER B 268 11.474 −34.121 −29.344 1.00 21.57 C ATOM 129 OG SER B 268 12.141 −35.316 −29.721 1.00 24.06 O ATOM 130 N GLU B 269 10.928 −31.563 −27.557 1.00 21.64 N ATOM 131 CA GLU B 269 10.282 −30.272 −27.378 1.00 21.95 C ATOM 132 C GLU B 269 11.321 −29.214 −26.999 1.00 21.68 C ATOM 133 O GLU B 269 11.301 −28.095 −27.518 1.00 18.12 O ATOM 134 CB GLU B 269 9.213 −30.399 −26.292 1.00 24.72 C ATOM 135 CG GLU B 269 8.480 −29.128 −25.940 1.00 27.67 C ATOM 136 CD GLU B 269 7.385 −29.380 −24.908 1.00 30.05 C ATOM 137 OE1 GLU B 269 6.325 −29.915 −25.287 1.00 31.50 O ATOM 138 OE2 GLU B 269 7.591 −29.057 −23.719 1.00 29.84 O ATOM 139 N ILE B 270 12.224 −29.581 −26.092 1.00 19.43 N ATOM 140 CA ILE B 270 13.295 −28.698 −25.638 1.00 20.62 C ATOM 141 C ILE B 270 14.214 −28.314 −26.806 1.00 20.58 C ATOM 142 O ILE B 270 14.595 −27.151 −26.954 1.00 20.50 O ATOM 143 CB ILE B 270 14.157 −29.391 −24.533 1.00 20.30 C ATOM 144 CG1 ILE B 270 13.337 −29.574 −23.254 1.00 21.32 C ATOM 145 CG2 ILE B 270 15.415 −28.595 −24.266 1.00 19.17 C ATOM 146 CD1 ILE B 270 12.926 −28.291 −22.583 1.00 23.40 C ATOM 147 N ALA B 277 19.316 −27.110 −21.396 1.00 17.01 N ATOM 148 CA ALA B 277 18.638 −27.807 −20.321 1.00 15.80 C ATOM 149 C ALA B 277 19.591 −28.526 −19.382 1.00 17.37 C ATOM 150 O ALA B 277 20.710 −28.891 −19.755 1.00 17.09 O ATOM 151 CB ALA B 277 17.641 −28.805 −20.895 1.00 17.01 C ATOM 152 N LEU B 278 19.147 −28.673 −18.138 1.00 17.14 N ATOM 153 CA LEU B 278 19.896 −29.429 −17.145 1.00 18.48 C ATOM 154 C LEU B 278 18.884 −30.535 −16.898 1.00 19.62 C ATOM 155 O LEU B 278 17.870 −30.330 −16.218 1.00 20.77 O ATOM 156 CB LEU B 278 20.140 −28.619 −15.869 1.00 19.19 C ATOM 157 CG LEU B 278 21.084 −29.308 −14.868 1.00 20.85 C ATOM 158 CD1 LEU B 278 21.283 −28.411 −13.668 1.00 21.11 C ATOM 159 CD2 LEU B 278 20.497 −30.647 −14.433 1.00 19.16 C ATOM 160 N PHE B 279 19.149 −31.691 −17.495 1.00 19.50 N ATOM 161 CA PHE B 279 18.266 −32.838 −17.392 1.00 21.59 C ATOM 162 C PHE B 279 18.525 −33.709 −16.167 1.00 22.86 C ATOM 163 O PHE B 279 19.671 −34.065 −15.871 1.00 23.32 O ATOM 164 CB PHE B 279 18.385 −33.700 −18.651 1.00 21.07 C ATOM 165 OG PHE B 279 17.740 −33.099 −19.876 1.00 19.35 C ATOM 166 CD1 PHE B 279 18.481 −32.898 −21.035 1.00 19.42 C ATOM 167 CD2 PHE B 279 16.379 −32.794 −19.888 1.00 18.16 C ATOM 168 CE1 PHE B 279 17.874 −32.405 −22.203 1.00 19.06 C ATOM 169 CE2 PHE B 279 15.759 −32.298 −21.052 1.00 17.65 C ATOM 170 CZ PHE B 279 16.515 −32.108 −22.208 1.00 15.61 C ATOM 171 N VAL B 280 17.445 −34.037 −15.461 1.00 23.88 N ATOM 172 CA VAL B 280 17.502 −34.902 −14.281 1.00 25.67 C ATOM 173 C VAL B 280 16.690 −36.136 −14.658 1.00 25.65 C ATOM 174 O VAL B 280 15.509 −36.239 −14.346 1.00 24.57 O ATOM 175 CB VAL B 280 16.883 −34.223 −13.048 1.00 26.89 C ATOM 176 CG1 VAL B 280 16.954 −35.159 −11.847 1.00 28.12 C ATOM 177 CG2 VAL B 280 17.631 −32.929 −12.742 1.00 27.70 C ATOM 178 N PRO B 281 17.324 −37.080 −15.370 1.00 27.08 N ATOM 179 CA PRO B 281 16.698 −38.320 −15.824 1.00 29.05 C ATOM 180 C PRO B 281 16.092 −39.121 −14.684 1.00 31.51 C ATOM 181 O PRO B 281 16.675 −39.223 −13.603 1.00 32.26 O ATOM 182 CB PRO B 281 17.851 −39.071 −16.492 1.00 29.44 C ATOM 183 CG PRO B 281 18.791 −37.992 −16.895 1.00 29.67 C ATOM 184 CD PRO B 281 18.750 −37.057 −15.726 1.00 27.31 C ATOM 185 N PHE B 282 14.908 −39.668 −14.923 1.00 33.83 N ATOM 186 CA PHE B 282 14.246 −40.496 −13.926 1.00 37.13 C ATOM 187 C PHE B 282 15.078 −41.776 −13.880 1.00 38.09 C ATOM 188 O PHE B 282 15.357 −42.373 −14.921 1.00 38.33 O ATOM 189 CB PHE B 282 12.818 −40.808 −14.372 1.00 38.38 C ATOM 190 CG PHE B 282 12.032 −41.606 −13.377 1.00 40.57 C ATOM 191 CD1 PHE B 282 11.720 −41.074 −12.130 1.00 41.80 C ATOM 192 CD2 PHE B 282 11.590 −42.886 −13.689 1.00 41.65 C ATOM 193 CE1 PHE B 282 10.975 −41.806 −11.209 1.00 42.03 C ATOM 194 CE2 PHE B 282 10.843 −43.628 −12.773 1.00 42.49 C ATOM 195 CZ PHE B 282 10.536 −43.085 −11.532 1.00 41.74 C ATOM 196 N GLN B 288 16.212 −45.321 −19.533 1.00 30.94 N ATOM 197 CA GLN B 288 15.622 −44.804 −20.755 1.00 30.77 C ATOM 198 C GLN B 288 15.783 −43.291 −20.885 1.00 29.70 C ATOM 199 O GLN B 288 16.268 −42.801 −21.902 1.00 29.79 O ATOM 200 CB GLN B 288 14.143 −45.158 −20.810 1.00 30.59 C ATOM 201 CG GLN B 288 13.473 −44.772 −22.109 1.00 29.73 C ATOM 202 CD GLN B 288 11.981 −44.971 −22.044 1.00 28.04 C ATOM 203 OE1 GLN B 288 11.294 −44.295 −21.279 1.00 29.59 O ATOM 204 NE2 GLN B 288 11.468 −45.905 −22.838 1.00 26.98 N ATOM 205 N GLN B 289 15.378 −42.554 −19.857 1.00 29.38 N ATOM 206 CA GLN B 289 15.474 −41.099 −19.904 1.00 29.46 C ATOM 207 C GLN B 289 16.906 −40.613 −20.005 1.00 29.36 C ATOM 208 O GLN B 289 17.173 −39.557 −20.585 1.00 29.12 O ATOM 209 CB GLN B 289 14.772 −40.472 −18.700 1.00 29.25 C ATOM 210 CG GLN B 289 13.265 −40.416 −18.883 1.00 29.32 C ATOM 211 CD GLN B 289 12.575 −39.585 −17.826 1.00 29.84 C ATOM 212 OE1 GLN B 289 13.191 −38.728 −17.188 1.00 29.52 O ATOM 213 NE2 GLN B 289 11.281 −39.821 −17.647 1.00 28.95 N ATOM 214 N TYR B 290 17.835 −41.374 −19.442 1.00 28.95 N ATOM 215 CA TYR B 290 19.228 −40.984 −19.550 1.00 29.55 C ATOM 216 C TYR B 290 19.593 −41.042 −21.032 1.00 28.80 C ATOM 217 O TYR B 290 20.192 −40.113 −21.567 1.00 29.22 O ATOM 218 CB TYR B 290 20.136 −41.934 −18.768 1.00 31.40 C ATOM 219 CG TYR B 290 21.587 −41.780 −19.148 1.00 33.37 C ATOM 220 CD1 TYR B 290 22.332 −40.682 −18.717 1.00 34.57 C ATOM 221 CD2 TYR B 290 22.192 −42.684 −20.017 1.00 34.90 C ATOM 222 CE1 TYR B 290 23.644 −40.490 −19.148 1.00 35.97 C ATOM 223 CE2 TYR B 290 23.497 −42.500 −20.453 1.00 36.03 C ATOM 224 CZ TYR B 290 24.214 −41.402 −20.019 1.00 36.29 C ATOM 225 OH TYR B 290 25.499 −41.215 −20.475 1.00 39.44 O ATOM 226 N ASN B 292 17.658 −40.779 −23.508 1.00 25.52 N ATOM 227 CA ASN B 292 16.902 −39.784 −24.270 1.00 26.06 C ATOM 228 C ASN B 292 17.605 −38.427 −24.258 1.00 25.99 C ATOM 229 O ASN B 292 17.566 −37.687 −25.244 1.00 26.18 O ATOM 230 CB ASN B 292 15.484 −39.599 −23.709 1.00 24.78 C ATOM 231 CG ASN B 292 14.590 −40.811 −23.928 1.00 24.46 C ATOM 232 OD1 ASN B 292 14.842 −41.641 −24.798 1.00 25.33 O ATOM 233 ND2 ASN B 292 13.523 −40.900 −23.146 1.00 23.83 N ATOM 234 N ALA B 293 18.242 −38.105 −23.139 1.00 25.66 N ATOM 235 CA ALA B 293 18.926 −36.822 −22.979 1.00 25.69 C ATOM 236 C ALA B 293 20.346 −36.800 −23.521 1.00 25.67 C ATOM 237 O ALA B 293 20.855 −35.743 −23.902 1.00 25.52 O ATOM 238 CB ALA B 293 18.940 −36.422 −21.506 1.00 24.17 C ATOM 239 N LEU B 296 21.375 −34.703 −26.688 1.00 25.66 N ATOM 240 CA LEU B 296 21.521 −33.265 −26.481 1.00 25.42 C ATOM 241 C LEU B 296 22.784 −32.935 −25.688 1.00 26.07 C ATOM 242 O LEU B 296 23.435 −31.917 −25.944 1.00 25.26 O ATOM 243 CB LEU B 296 20.283 −32.685 −25.779 1.00 24.45 C ATOM 244 CG LEU B 296 19.066 −32.458 −26.679 1.00 25.59 C ATOM 245 CD1 LEU B 296 17.968 −31.718 −25.911 1.00 23.56 C ATOM 246 CD2 LEU B 296 19.496 −31.630 −27.893 1.00 25.87 C ATOM 247 N ALA B 302 23.066 −29.504 −23.507 1.00 20.94 N ATOM 248 CA ALA B 302 22.516 −29.770 −22.186 1.00 21.78 C ATOM 249 C ALA B 302 23.503 −30.507 −21.288 1.00 22.69 C ATOM 250 O ALA B 302 24.561 −30.948 −21.739 1.00 22.25 O ATOM 251 CB ALA B 302 21.243 −30.595 −22.327 1.00 20.10 C ATOM 252 N LYS B 303 23.156 −30.613 −20.009 1.00 24.62 N ATOM 253 CA LYS B 303 23.979 −31.340 −19.048 1.00 25.86 C ATOM 254 C LYS B 303 23.083 −32.319 −18.302 1.00 26.41 C ATOM 255 O LYS B 303 22.015 −31.948 −17.802 1.00 25.76 O ATOM 256 CB LYS B 303 24.632 −30.401 −18.036 1.00 27.85 C ATOM 257 CG LYS B 303 25.466 −31.146 −16.986 1.00 29.37 C ATOM 258 CD LYS B 303 26.150 −30.186 −16.025 1.00 32.41 C ATOM 259 CE LYS B 303 27.083 −30.912 −15.056 1.00 33.22 C ATOM 260 NZ LYS B 303 27.827 −29.952 −14.181 1.00 33.62 N ATOM 261 N ILE B 304 23.520 −33.570 −18.234 1.00 25.65 N ATOM 262 CA ILE B 304 22.753 −34.598 −17.550 1.00 27.17 C ATOM 263 C ILE B 304 23.308 −34.855 −16.160 1.00 27.00 C ATOM 264 O ILE B 304 24.511 −35.012 −15.986 1.00 27.46 O ATOM 265 CB ILE B 304 22.786 −35.946 −18.316 1.00 27.06 C ATOM 266 CG1 ILE B 304 22.242 −35.769 −19.733 1.00 27.61 C ATOM 267 CG2 ILE B 304 21.977 −36.996 −17.555 1.00 28.49 C ATOM 268 CD1 ILE B 304 22.380 −37.009 −20.599 1.00 27.05 C ATOM 269 N ILE B 305 22.428 −34.869 −15.168 1.00 27.22 N ATOM 270 CA ILE B 305 22.843 −35.178 −13.813 1.00 29.01 C ATOM 271 C ILE B 305 21.934 −36.302 −13.351 1.00 29.64 C ATOM 272 O ILE B 305 20.806 −36.067 −12.932 1.00 29.25 O ATOM 273 CB ILE B 305 22.713 −33.977 −12.858 1.00 28.91 C ATOM 274 CD1 ILE B 305 23.660 −32.855 −13.299 1.00 29.51 C ATOM 275 CD2 ILE B 305 23.063 −34.416 −11.432 1.00 30.98 C ATOM 276 CD1 ILE B 305 23.674 −31.653 −12.367 1.00 29.43 C TER

TABLE 5 ATOMIC COORDINATES OF ACCEPTOR BINDING SITE REMARK 4 1MUR COMPLIES WITH FORMAT V. 2.0, MAY 11, 2000 ATOM 1 N MET B 12 −0.734 −48.902 −33.817 1.00 23.68 N ATOM 2 CA MET B 12 −0.523 −49.707 −32.613 1.00 24.54 C ATOM 3 C MET B 12 0.361 −48.840 −31.720 1.00 25.31 C ATOM 4 O MET B 12 1.546 −48.645 −32.006 1.00 23.88 O ATOM 5 CB MET B 12 0.192 −51.019 −32.971 1.00 24.28 C ATOM 6 CG MET B 12 −0.402 −51.726 −34.188 1.00 25.19 C ATOM 7 SD MET B 12 0.399 −53.284 −34.669 1.00 26.54 S ATOM 8 CE MET B 12 1.990 −52.691 −35.289 1.00 22.99 C ATOM 9 N ALA B 13 −0.224 −48.292 −30.657 1.00 27.08 N ATOM 10 CA ALA B 13 0.508 −47.410 −29.752 1.00 29.43 C ATOM 11 C ALA B 13 −0.239 −47.192 −28.436 1.00 31.80 C ATOM 12 O ALA B 13 −1.143 −46.350 −28.352 1.00 32.16 O ATOM 13 CB ALA B 13 0.747 −46.074 −30.429 1.00 28.82 C ATOM 14 N GLY B 14 0.150 −47.934 −27.405 1.00 32.46 N ATOM 15 CA GLY B 14 −0.513 −47.804 −26.120 1.00 33.82 C ATOM 16 C GLY B 14 −0.107 −46.595 −25.299 1.00 34.82 C ATOM 17 O GLY B 14 0.975 −46.040 −25.479 1.00 35.47 O ATOM 18 N GLY B 15 −0.986 −46.188 −24.385 1.00 35.56 N ATOM 19 CA GLY B 15 −0.700 −45.047 −23.536 1.00 36.08 C ATOM 20 C GLY B 15 0.539 −45.254 −22.683 1.00 36.84 C ATOM 21 O GLY B 15 1.293 −44.311 −22.426 1.00 36.03 O ATOM 22 N THR B 16 0.755 −46.488 −22.240 1.00 36.65 N ATOM 23 CA THR B 16 1.920 −46.787 −21.421 1.00 38.51 C ATOM 24 C THR B 16 3.158 −46.497 −22.264 1.00 38.35 C ATOM 25 O THR B 16 3.191 −46.798 −23.460 1.00 39.90 O ATOM 26 CB THR B 16 1.926 −48.258 −20.974 1.00 38.51 C ATOM 27 CG1 THR B 16 0.686 −48.558 −20.321 1.00 38.39 O ATOM 28 CG2 THR B 16 3.075 −48.518 −20.005 1.00 39.11 C ATOM 29 N GLY B 17 4.168 −45.897 −21.649 1.00 37.68 N ATOM 30 CA GLY B 17 5.367 −45.567 −22.392 1.00 36.57 C ATOM 31 C GLY B 17 5.161 −44.303 −23.211 1.00 35.56 C ATOM 32 O GLY B 17 6.079 −43.843 −23.890 1.00 35.03 O ATOM 33 N GLY B 18 3.949 −43.752 −23.150 1.00 33.83 N ATOM 34 CA GLY B 18 3.631 −42.529 −23.872 1.00 33.48 C ATOM 35 C GLY B 18 3.825 −42.593 −25.378 1.00 33.12 C ATOM 36 O GLY B 18 4.345 −41.650 −25.984 1.00 35.38 O ATOM 37 N HIS B 19 3.416 −43.699 −25.988 1.00 30.26 N ATOM 38 CA HIS B 19 3.548 −43.865 −27.435 1.00 28.22 C ATOM 39 C HIS B 19 2.280 −43.370 −28.144 1.00 27.91 C ATOM 40 O HIS B 19 2.300 −43.049 −29.337 1.00 26.91 O ATOM 41 CB HIS B 19 3.772 −45.349 −27.779 1.00 25.81 C ATOM 42 CG HIS B 19 4.957 −45.966 −27.094 1.00 25.35 C ATOM 43 ND1 HIS B 19 4.845 −47.025 −26.217 1.00 24.57 N ATOM 44 CD2 HIS B 19 6.281 −45.694 −27.184 1.00 24.18 C ATOM 45 CE1 HIS B 19 6.046 −47.380 −25.798 1.00 23.08 C ATOM 46 NE2 HIS B 19 6.936 −46.589 −26.369 1.00 25.51 N ATOM 47 N VAL B 20 1.180 −43.310 −27.402 1.00 27.65 N ATOM 48 CA VAL B 20 −0.098 −42.894 −27.965 1.00 27.77 C ATOM 49 C VAL B 20 −0.140 −41.452 −28.470 1.00 27.57 C ATOM 50 O VAL B 20 −0.771 −41.172 −29.486 1.00 27.12 O ATOM 51 CB VAL B 20 −1.248 −43.080 −26.942 1.00 28.57 C ATOM 52 CG1 VAL B 20 −1.082 −42.114 −25.787 1.00 30.03 C ATOM 53 CG2 VAL B 20 −2.602 −42.873 −27.631 1.00 26.82 C ATOM 54 N LEU B 40 −5.323 −50.004 −32.549 1.00 25.21 N ATOM 55 CA LEU B 40 −5.200 −51.364 −32.026 1.00 24.71 C ATOM 56 C LEU B 40 −4.535 −51.235 −30.655 1.00 23.33 C ATOM 57 O LEU B 40 −3.387 −50.824 −30.563 1.00 23.43 O ATOM 58 CB LEU B 40 −4.326 −52.221 −32.952 1.00 25.21 C ATOM 59 CG LEU B 40 −4.416 −53.754 −32.868 1.00 26.95 C ATOM 60 CD1 LEU B 40 −3.037 −54.334 −32.571 1.00 27.63 C ATOM 61 CD2 LEU B 40 −5.421 −54.179 −31.817 1.00 26.69 C ATOM 62 N GLU B 47 −4.976 −45.941 −23.678 1.00 32.85 N ATOM 63 CA GLU B 47 −5.458 −45.655 −25.029 1.00 31.79 C ATOM 64 C GLU B 47 −6.938 −46.017 −25.191 1.00 31.81 C ATOM 65 O GLU B 47 −7.626 −45.476 −26.055 1.00 31.31 O ATOM 66 CB GLU B 47 −4.624 −46.402 −26.080 1.00 30.62 C ATOM 67 CG GLU B 47 −4.755 −47.922 −26.051 1.00 29.85 C ATOM 68 CD GLU B 47 −3.793 −48.597 −25.082 1.00 29.78 C ATOM 69 OE1 GLU B 47 −3.188 −47.895 −24.247 1.00 28.76 O ATOM 70 OE2 GLU B 47 −3.649 −49.840 −25.156 1.00 29.01 O ATOM 71 N ILE B 63 −3.428 −59.342 −24.313 1.00 30.07 N ATOM 72 CA ILE B 63 −2.036 −59.770 −24.231 1.00 31.38 C ATOM 73 C ILE B 63 −1.623 −59.981 −22.775 1.00 33.08 C ATOM 74 O ILE B 63 −0.444 −59.872 −22.430 1.00 33.21 O ATOM 75 CB ILE B 63 −1.081 −58.745 −24.883 1.00 30.06 C ATOM 76 CG1 ILE B 63 −1.143 −57.411 −24.137 1.00 29.94 C ATOM 77 CG2 ILE B 63 −1.442 −58.567 −26.353 1.00 30.41 C ATOM 78 CD1 ILE B 63 −0.128 −56.384 −24.632 1.00 29.62 C ATOM 79 N ARG B 67 2.953 −59.185 −21.440 1.00 31.54 N ATOM 80 CA ARG B 67 3.671 −57.928 −21.277 1.00 30.90 C ATOM 81 C ARG B 67 5.071 −58.142 −20.713 1.00 29.99 C ATOM 82 O ARG B 67 5.294 −59.034 −19.889 1.00 28.67 O ATOM 83 CB ARG B 67 2.888 −56.984 −20.363 1.00 32.28 C ATOM 84 CC ARG B 67 1.540 −56.576 −20.913 1.00 34.65 C ATOM 85 CD ARG B 67 0.926 −55.440 −20.097 1.00 36.69 C ATOM 86 NE ARG B 67 −0.259 −54.889 −20.748 1.00 38.28 N ATOM 87 CZ ARG B 67 −1.425 −55.519 −20.853 1.00 39.05 C ATOM 88 NH1 ARG B 67 −1.583 −56.734 −20.341 1.00 39.61 N ATOM 89 NH2 ARG B 67 −2.434 −54.935 −21.487 1.00 39.52 N ATOM 90 N GLY B 68 6.014 −57.321 −21.165 1.00 27.75 N ATOM 91 CA GLY B 68 7.380 −57.427 −20.685 1.00 26.79 C ATOM 92 C GLY B 68 8.166 −58.579 −21.280 1.00 25.41 C ATOM 93 O GLY B 68 9.326 −58.779 −20.943 1.00 26.04 O ATOM 94 N GLY B 102 3.556 −48.986 −35.936 1.00 20.96 N ATOM 95 CA GLY B 102 3.796 −49.357 −34.549 1.00 19.23 C ATOM 96 C GLY B 102 4.655 −48.282 −33.918 1.00 18.45 C ATOM 97 O GLY B 102 5.765 −48.016 −34.381 1.00 18.70 O ATOM 98 N MET B 103 4.155 −47.660 −32.857 1.00 18.01 N ATOM 99 CA MET B 103 4.892 −46.597 −32.191 1.00 18.93 C ATOM 100 C MET B 103 5.612 −47.128 −30.957 1.00 18.98 C ATOM 101 O MET B 103 6.134 −46.357 −30.158 1.00 17.96 O ATOM 102 CB MET B 103 3.928 −45.477 −31.781 1.00 20.02 C ATOM 103 CG MET B 103 3.121 −44.888 −32.944 1.00 21.61 C ATOM 104 SD MET B 103 4.212 −44.135 −34.157 1.00 23.45 S ATOM 105 CE MET B 103 4.718 −42.680 −33.271 1.00 21.40 C ATOM 106 N GLY B 104 5.640 −48.450 −30.827 1.00 21.56 N ATOM 107 CA GLY B 104 6.275 −49.080 −29.686 1.00 21.89 C ATOM 108 C GLY B 104 5.192 −49.614 −28.764 1.00 23.28 C ATOM 109 O GLY B 104 4.009 −49.353 −28.980 1.00 22.50 O ATOM 110 N GLY B 105 5.583 −50.364 −27.741 1.00 23.01 N ATOM 111 CA GLY B 105 4.593 −50.905 −26.827 1.00 23.54 C ATOM 112 C GLY B 105 4.358 −52.380 −27.078 1.00 23.17 C ATOM 113 O GLY B 105 4.449 −52.844 −28.214 1.00 22.69 O ATOM 114 N TYR B 106 4.018 −53.118 −26.026 1.00 22.87 N ATOM 115 CA TYR B 106 3.818 −54.554 −26.159 1.00 22.37 C ATOM 116 C TYR B 106 2.719 −55.018 −27.100 1.00 20.52 C ATOM 117 O TYR B 106 2.867 −56.052 −27.746 1.00 20.50 O ATOM 118 CB TYR B 106 3.632 −55.181 −24.774 1.00 25.08 C ATOM 119 CG TYR B 106 4.864 −55.008 −23.929 1.00 28.19 C ATOM 120 CD1 TYR B 106 4.869 −54.153 −22.830 1.00 31.96 C ATOM 121 CD2 TYR B 106 6.058 −55.631 −24.282 1.00 31.27 C ATOM 122 CE1 TYR B 106 6.043 −53.915 −22.108 1.00 33.13 C ATOM 123 CE2 TYR B 106 7.234 −55.400 −23.569 1.00 32.27 C ATOM 124 CZ TYR B 106 7.219 −54.541 −22.487 1.00 33.19 C ATOM 125 OH TYR B 106 8.388 −54.291 −21.802 1.00 35.95 O ATOM 126 N VAL B 107 1.628 −54.270 −27.205 1.00 19.06 N ATOM 127 CA VAL B 107 0.557 −54.694 −28.099 1.00 18.06 C ATOM 128 C VAL B 107 1.015 −54.743 −29.559 1.00 17.45 C ATOM 129 O VAL B 107 0.502 −55.536 −30.346 1.00 16.99 O ATOM 130 CB VAL B 107 −0.690 −53.774 −27.978 1.00 20.95 C ATOM 131 CG1 VAL B 107 −0.407 −52.407 −28.589 1.00 21.39 C ATOM 132 CG2 VAL B 107 −1.879 −54.433 −28.658 1.00 21.30 C ATOM 133 N SER B 108 1.991 −53.916 −29.918 1.00 17.96 N ATOM 134 CA SER B 108 2.488 −53.892 −31.290 1.00 19.67 C ATOM 135 C SER B 108 3.197 −55.187 −31.694 1.00 20.38 C ATOM 136 O SER B 108 3.385 −55.449 −32.884 1.00 21.25 O ATOM 137 CB SER B 108 3.424 −52.691 −31.508 1.00 19.56 C ATOM 138 OG SER B 108 4.666 −52.824 −30.837 1.00 19.63 O ATOM 139 N GLY B 109 3.595 −55.995 −30.710 1.00 19.59 N ATOM 140 CA GLY B 109 4.251 −57.256 −31.023 1.00 20.03 C ATOM 141 C GLY B 109 3.311 −58.170 −31.792 1.00 19.61 C ATOM 142 O GLY B 109 3.579 −58.517 −32.940 1.00 19.24 O ATOM 143 N PRO B 110 2.206 −58.606 −31.173 1.00 19.20 N ATOM 144 CA PRO B 110 1.251 −59.478 −31.855 1.00 18.99 C ATOM 145 C PRO B 110 0.651 −58.761 −33.075 1.00 19.22 C ATOM 146 O PRO B 110 0.406 −59.371 −34.116 1.00 17.13 O ATOM 147 CB PRO B 110 0.198 −59.737 −30.778 1.00 20.41 C ATOM 148 CG PRO B 110 0.998 −59.720 −29.515 1.00 19.81 C ATOM 149 CD PRO B 110 1.914 −58.528 −29.729 1.00 19.94 C ATOM 150 N HIS B 125 8.182 −46.638 −35.447 1.00 21.40 N ATOM 151 CA HIS B 125 8.814 −45.413 −34.981 1.00 21.42 C ATOM 152 C HIS B 125 9.196 −45.642 −33.519 1.00 21.70 C ATOM 153 O HIS B 125 8.378 −46.117 −32.725 1.00 19.81 O ATOM 154 CB HIS B 125 7.858 −44.218 −35.067 1.00 21.57 C ATOM 155 CG HIS B 125 8.432 −42.948 −34.511 1.00 23.73 C ATOM 156 ND1 HIS B 125 9.274 −42.127 −35.236 1.00 26.23 N ATOM 157 CD2 HIS B 125 8.300 −42.368 −33.295 1.00 22.15 C ATOM 158 CE1 HIS B 125 9.631 −41.095 −34.490 1.00 24.20 C ATOM 159 NE2 HIS B 125 9.054 −41.218 −33.307 1.00 26.07 N ATOM 160 N GLU B 126 10.444 −45.332 −33.186 1.00 21.20 N ATOM 161 CA GLU B 126 10.947 −45.452 −31.817 1.00 22.15 C ATOM 162 C GLU B 126 11.205 −44.027 −31.326 1.00 21.93 C ATOM 163 O GLU B 126 12.016 −43.300 −31.908 1.00 21.33 O ATOM 164 CB GLU B 126 12.252 −46.246 −31.790 1.00 21.99 C ATOM 165 CG GLU B 126 12.958 −46.206 −30.439 1.00 22.04 C ATOM 166 CD GLU B 126 12.119 −46.824 −29.338 1.00 21.43 C ATOM 167 OE1 GLU B 126 11.767 −48.014 −29.471 1.00 21.92 O ATOM 168 OE2 GLU B 126 11.807 −46.124 −28.349 1.00 21.08 O ATOM 169 N GLN B 127 10.520 −43.624 −30.259 1.00 22.62 N ATOM 170 CA GLN B 127 10.682 −42.270 −29.735 1.00 22.81 C ATOM 171 C GLN B 127 11.874 −42.087 −28.809 1.00 22.39 C ATOM 172 O GLN B 127 12.399 −40.976 −28.682 1.00 22.43 O ATOM 173 CB GLN B 127 9.414 −41.814 −28.989 1.00 23.56 C ATOM 174 CG GLN B 127 8.147 −41.783 −29.830 1.00 24.46 C ATOM 175 CD GLN B 127 7.312 −43.041 −29.687 1.00 25.85 C ATOM 176 OE1 GLN B 127 6.842 −43.366 −28.591 1.00 23.78 O ATOM 177 NE2 GLN B 127 7.119 −43.758 −30.797 1.00 24.91 N ATOM 178 N ASN B 128 12.314 −43.173 −28.177 1.00 22.35 N ATOM 179 CA ASN B 128 13.406 −43.097 −27.216 1.00 22.96 C ATOM 180 C ASN B 128 14.824 −43.314 −27.742 1.00 23.87 C ATOM 181 O ASN B 128 15.026 −43.856 −28.830 1.00 24.05 O ATOM 182 CB ASN B 128 13.136 −44.080 −26.064 1.00 22.85 C ATOM 183 CG ASN B 128 11.742 −43.919 −25.474 1.00 23.25 C ATOM 184 OD1 ASN B 128 10.804 −44.632 −25.848 1.00 26.04 O ATOM 185 ND2 ASN B 128 11.597 −42.975 −24.556 1.00 22.68 N ATOM 186 N GLY B 132 12.851 −49.814 −27.506 1.00 24.52 N ATOM 187 CA GLY B 132 12.007 −50.532 −26.568 1.00 24.05 C ATOM 188 C GLY B 132 12.150 −52.019 −26.831 1.00 23.35 C ATOM 189 O GLY B 132 12.582 −52.419 −27.904 1.00 22.89 O ATOM 190 N LEU B 133 11.788 −52.846 −25.860 1.00 23.38 N ATOM 191 CA LEU B 133 11.903 −54.293 −26.020 1.00 24.54 C ATOM 192 C LEU B 133 11.209 −54.833 −27.276 1.00 22.84 C ATOM 193 O LEU B 133 11.784 −55.619 −28.027 1.00 21.86 O ATOM 194 CB LEU B 133 11.328 −54.996 −24.786 1.00 25.48 C ATOM 195 CG LEU B 133 11.388 −56.527 −24.780 1.00 27.50 C ATOM 196 CD1 LEU B 133 12.840 −56.984 −24.866 1.00 28.69 C ATOM 197 CD2 LEU B 133 10.735 −57.059 −23.509 1.00 28.04 C ATOM 198 N THR B 134 9.975 −54.401 −27.499 1.00 21.72 N ATOM 199 CA THR B 134 9.202 −54.860 −28.639 1.00 21.22 C ATOM 200 C THR B 134 9.693 −54.326 −29.986 1.00 20.62 C ATOM 201 O THR B 134 9.843 −55.091 −30.932 1.00 20.33 O ATOM 202 CB THR B 134 7.716 −54.509 −28.449 1.00 20.99 C ATOM 203 OG1 THR B 134 7.257 −55.075 −27.210 1.00 20.94 O ATOM 204 CG2 THR B 134 6.872 −55.073 −29.600 1.00 20.64 C ATOM 205 N ASN B 135 9.932 −53.021 −30.075 1.00 21.24 N ATOM 206 CA ASN B 135 10.407 −52.419 −31.324 1.00 20.50 C ATOM 207 C ASN B 135 11.724 −53.064 −31.767 1.00 20.78 C ATOM 208 O ASN B 135 11.945 −53.290 −32.953 1.00 20.41 O ATOM 209 CB ASN B 135 10.637 −50.911 −31.142 1.00 19.58 C ATOM 210 CG ASN B 135 9.457 −50.058 −31.597 1.00 19.93 C ATOM 211 OD1 ASN B 135 9.454 −48.837 −31.390 1.00 21.78 O ATOM 212 ND2 ASN B 135 8.467 −50.677 −32.219 1.00 17.21 N ATOM 213 N LEU B 138 10.741 −56.381 −33.386 1.00 21.61 N ATOM 214 CA LEU B 138 9.744 −56.188 −34.431 1.00 23.15 C ATOM 215 C LEU B 138 10.384 −55.558 −35.676 1.00 23.07 C ATOM 216 O LEU B 138 9.958 −55.801 −36.809 1.00 22.68 O ATOM 217 CB LEU B 138 8.618 −55.305 −33.886 1.00 23.87 C ATOM 218 CG LEU B 138 7.312 −55.155 −34.664 1.00 26.48 C ATOM 219 CD1 LEU B 138 6.672 −56.508 −34.915 1.00 25.34 C ATOM 220 CD2 LEU B 138 6.383 −54.267 −33.851 1.00 25.90 C TER

TABLE 6 ATOMIC COORDINATES OF MEMBRANE ASSOCIATION SITE REMARK 4 1MUR COMPLIES WITH FORMAT V. 2.0, MAY 11, 2000 ATOM 1 N MET B 12 −0.734 −48.902 −33.817 1.00 23.68 N ATOM 2 CA MET B 12 −0.523 −49.707 −32.613 1.00 24.54 C ATOM 3 C MET B 12 0.361 −48.840 −31.720 1.00 25.31 C ATOM 4 O MET B 12 1.546 −48.645 −32.006 1.00 23.88 O ATOM 5 CB MET B 12 0.192 −51.019 −32.971 1.00 24.28 C ATOM 6 CG MET B 12 −0.402 −51.726 −34.188 1.00 25.19 C ATOM 7 SD MET B 12 0.399 −53.284 −34.669 1.00 26.54 S ATOM 8 CE MET B 12 1.990 −52.691 −35.289 1.00 22.99 C ATOM 9 N LEU B 40 −5.323 −50.004 −32.549 1.00 25.21 N ATOM 10 CA LEU B 40 −5.200 −51.364 −32.026 1.00 24.71 C ATOM 11 C LEU B 40 −4.535 −51.235 −30.655 1.00 23.33 C ATOM 12 O LEU B 40 −3.387 −50.824 −30.563 1.00 23.43 O ATOM 13 CB LEU B 40 −4.326 −52.221 −32.952 1.00 25.21 C ATOM 14 CG LEU B 40 −4.416 −53.754 −32.868 1.00 26.95 C ATOM 15 CD1 LEU B 40 −3.037 −54.334 −32.571 1.00 27.63 C ATOM 16 CD2 LEU B 40 −5.421 −54.179 −31.817 1.00 26.69 C ATOM 17 N ILE B 61 −7.271 −56.229 −28.295 1.00 29.38 N ATOM 18 CA ILE B 61 −6.832 −57.616 −28.269 1.00 28.55 C ATOM 19 C ILE B 61 −6.344 −57.855 −26.848 1.00 29.13 C ATOM 20 O ILE B 61 −6.124 −56.906 −26.091 1.00 28.80 O ATOM 21 CB ILE B 61 −5.674 −57.923 −29.258 1.00 28.48 C ATOM 22 CG1 ILE B 61 −4.422 −57.126 −28.892 1.00 26.70 C ATOM 23 CG2 ILE B 61 −6.123 −57.650 −30.694 1.00 27.65 C ATOM 24 CD1 ILE B 61 −3.177 −57.615 −29.638 1.00 27.03 C ATOM 25 N ARG B 62 −6.186 −59.116 −26.473 1.00 29.38 N ATOM 26 CA ARG B 62 −5.709 −59.416 −25.133 1.00 30.76 C ATOM 27 C ARG B 62 −4.274 −59.923 −25.156 1.00 29.32 C ATOM 28 O ARG B 62 −3.933 −60.809 −25.934 1.00 28.65 O ATOM 29 CB ARG B 62 −6.630 −60.447 −24.461 1.00 32.36 C ATOM 30 CG ARG B 62 −6.130 −60.955 −23.114 1.00 35.99 C ATOM 31 CD ARG B 62 −5.438 −59.859 −22.311 1.00 37.86 C ATOM 32 NE ARG B 62 −6.297 −58.718 −22.004 1.00 40.01 N ATOM 33 CZ ARG B 62 −5.840 −57.504 −21.711 1.00 39.09 C ATOM 34 NH1 ARG B 62 −4.536 −57.275 −21.690 1.00 39.24 N ATOM 35 NH2 ARG B 62 −6.686 −56.518 −21.439 1.00 40.03 N ATOM 36 N ILE B 63 −3.428 −59.342 −24.313 1.00 30.07 N ATOM 37 CA ILE B 63 −2.036 −59.770 −24.231 1.00 31.38 C ATOM 38 C ILE B 63 −1.623 −59.981 −22.775 1.00 33.08 C ATOM 39 O ILE B 63 −0.444 −59.872 −22.430 1.00 33.21 O ATOM 40 CB ILE B 63 −1.081 −58.745 −24.883 1.00 30.06 C ATOM 41 CG1 ILE B 63 −1.143 −57.411 −24.137 1.00 29.94 C ATOM 42 CG2 ILE B 63 −1.442 −58.567 −26.353 1.00 30.41 C ATOM 43 CD1 ILE B 63 −0.128 −56.384 −24.632 1.00 29.62 C ATOM 44 N SER B 64 −2.603 −60.284 −21.927 1.00 35.38 N ATOM 45 CA SER B 64 −2.356 −60.520 −20.505 1.00 37.51 C ATOM 46 C SER B 64 −1.326 −61.622 −20.311 1.00 37.32 C ATOM 47 O SER B 64 −1.411 −62.682 −20.933 1.00 37.86 O ATOM 48 CB SER B 64 −3.652 −60.912 −19.792 1.00 38.82 C ATOM 49 OG SER B 64 −4.558 −59.823 −19.750 1.00 42.88 O ATOM 50 N GLY B 65 −0.356 −61.370 −19.441 1.00 37.81 N ATOM 51 CA GLY B 65 0.679 −62.355 −19.199 1.00 37.13 C ATOM 52 C GLY B 65 1.798 −62.283 −20.226 1.00 36.76 C ATOM 53 O GLY B 65 2.858 −62.889 −20.038 1.00 37.57 O ATOM 54 N LEU B 66 1.577 −61.539 −21.307 1.00 34.63 N ATOM 55 CA LEU B 66 2.591 −61.413 −22.355 1.00 33.17 C ATOM 56 C LEU B 66 3.414 −60.133 −22.246 1.00 32.72 C ATOM 57 O LEU B 66 4.451 −60.002 −22.893 1.00 33.13 O ATOM 58 CB LEU B 66 1.936 −61.470 −23.735 1.00 32.08 C ATOM 59 CG LEU B 66 1.162 −62.747 −24.061 1.00 32.52 C ATOM 60 CD1 LEU B 66 0.563 −62.626 −25.445 1.00 31.38 C ATOM 61 CD2 LEU B 66 2.093 −63.957 −23.984 1.00 31.67 C ATOM 62 N ARG B 67 2.953 −59.185 −21.440 1.00 31.54 N ATOM 63 CA ARG B 67 3.671 −57.928 −21.277 1.00 30.90 C ATOM 64 C ARG B 67 5.071 −58.142 −20.713 1.00 29.99 C ATOM 65 O ARG B 67 5.294 −59.034 −19.889 1.00 28.67 O ATOM 66 CB ARG B 67 2.888 −56.984 −20.363 1.00 32.28 C ATOM 67 CG ARG B 67 1.540 −56.576 −20.913 1.00 34.65 C ATOM 68 CD ARG B 67 0.926 −55.440 −20.097 1.00 36.69 C ATOM 69 NE ARG B 67 −0.259 −54.889 −20.748 1.00 38.28 N ATOM 70 CZ ARG B 67 −1.425 −55.519 −20.853 1.00 39.05 C ATOM 71 NH1 ARG B 67 −1.583 −56.734 −20.341 1.00 39.61 N ATOM 72 NH2 ARG B 67 −2.434 −54.935 −21.487 1.00 39.52 N ATOM 73 N GLY B 68 6.014 −57.321 −21.165 1.00 27.75 N ATOM 74 CA GLY B 68 7.380 −57.427 −20.685 1.00 26.79 C ATOM 75 C GLY B 68 8.166 −58.579 −21.280 1.00 25.41 C ATOM 76 O GLY B 68 9.326 −58.779 −20.943 1.00 26.04 O ATOM 77 N LYS B 69 7.546 −59.342 −22.170 1.00 24.55 N ATOM 78 CA LYS B 69 8.238 −60.463 −22.796 1.00 23.93 C ATOM 79 G LYS B 69 8.825 −60.062 −24.142 1.00 23.32 C ATOM 80 O LYS B 69 8.151 −59.404 −24.944 1.00 21.96 O ATOM 81 CB LYS B 69 7.284 −61.641 −23.033 1.00 24.12 C ATOM 82 CG LYS B 69 6.757 −62.360 −21.794 1.00 25.08 C ATOM 83 CD LYS B 69 5.887 −63.553 −22.224 1.00 25.44 C ATOM 84 CE LYS B 69 5.357 −64.358 −21.035 1.00 28.31 C ATOM 85 NZ LYS B 69 6.468 −64.877 −20.175 1.00 29.71 N ATOM 86 N GLY B 70 10.075 −60.470 −24.374 1.00 22.48 N ATOM 87 CA GLY B 70 10.755 −60.229 −25.636 1.00 22.26 C ATOM 88 C GLY B 70 10.308 −61.337 −26.588 1.00 22.17 C ATOM 89 O GLY B 70 9.512 −62.183 −26.195 1.00 21.62 O ATOM 90 N ILE B 71 10.819 −61.373 −27.814 1.00 21.85 N ATOM 91 CA ILE B 71 10.357 −62.386 −28.762 1.00 23.55 C ATOM 92 C ILE B 71 10.616 −63.840 −28.359 1.00 23.88 C ATOM 93 O ILE B 71 9.775 −64.707 −28.592 1.00 21.66 O ATOM 94 CB ILE B 71 10.926 −62.142 −30.181 1.00 23.52 C ATOM 95 CG1 ILE B 71 10.264 −63.096 −31.182 1.00 24.18 C ATOM 96 CG2 ILE B 71 12.435 −62.375 −30.192 1.00 25.96 C ATOM 97 CD1 ILE B 71 8.745 −62.981 −31.263 1.00 25.73 C ATOM 98 N LYS B 72 11.764 −64.119 −27.751 1.00 23.82 N ATOM 99 CA LYS B 72 12.038 −65.491 −27.343 1.00 24.92 C ATOM 100 G LYS B 72 11.068 −65.925 −26.245 1.00 23.73 C ATOM 101 O LYS B 72 10.592 −67.062 −26.245 1.00 24.08 O ATOM 102 CB LYS B 72 13.491 −65.634 −26.875 1.00 26.86 C ATOM 103 CG LYS B 72 14.496 −65.590 −28.019 1.00 31.29 C ATOM 104 CD LYS B 72 15.925 −65.791 −27.518 1.00 36.00 C ATOM 105 CE LYS B 72 16.926 −65.816 −28.671 1.00 38.82 C ATOM 106 NZ LYS B 72 18.342 −65.957 −28.192 1.00 41.21 N ATOM 107 N ALA B 73 10.765 −65.016 −25.322 1.00 21.62 N ATOM 108 CA ALA B 73 9.839 −65.306 −24.233 1.00 21.18 C ATOM 109 C ALA B 73 8.412 −65.454 −24.771 1.00 20.36 C ATOM 110 O ALA B 73 7.619 −66.250 −24.267 1.00 18.97 O ATOM 111 CB ALA B 73 9.895 −64.196 −23.187 1.00 22.25 C ATOM 112 N LEU B 74 8.076 −64.673 −25.791 1.00 20.23 N ATOM 113 CA LEU B 74 6.745 −64.762 −26.387 1.00 19.36 C ATOM 114 C LEU B 74 6.549 −66.110 −27.069 1.00 19.37 C ATOM 115 O LEU B 74 5.539 −66.779 −26.863 1.00 20.01 O ATOM 116 CB LEU B 74 6.540 −63.643 −27.417 1.00 18.42 C ATOM 117 CG LEU B 74 6.422 −62.208 −26.884 1.00 18.80 C ATOM 118 CD1 LEU B 74 6.473 −61.197 −28.039 1.00 19.86 C ATOM 119 CD2 LEU B 74 5.109 −62.071 −26.104 1.00 19.45 C ATOM 120 N ILE B 75 7.520 −66.507 −27.883 1.00 20.59 N ATOM 121 CA ILE B 75 7.434 −67.768 −28.601 1.00 21.18 C ATOM 122 C ILE B 75 7.488 −68.942 −27.624 1.00 21.20 C ATOM 123 O ILE B 75 7.125 −70.063 −27.979 1.00 21.59 O ATOM 124 CB ILE B 75 8.571 −67.896 −29.641 1.00 22.95 C ATOM 125 CG1 ILE B 75 8.598 −66.657 −30.540 1.00 26.82 C ATOM 126 CG2 ILE B 75 8.334 −69.108 −30.527 1.00 25.38 C ATOM 127 CD1 ILE B 75 7.304 −66.442 −31.327 1.00 28.48 C ATOM 128 N ALA B 76 7.940 −68.680 −26.399 1.00 20.49 N ATOM 129 CA ALA B 76 7.996 −69.726 −25.374 1.00 21.72 C ATOM 130 C ALA B 76 6.624 −69.904 −24.732 1.00 21.54 C ATOM 131 O ALA B 76 6.441 −70.778 −23.875 1.00 20.75 O ATOM 132 CB ALA B 76 9.026 −69.372 −24.305 1.00 21.92 C ATOM 133 N ALA B 77 5.668 −69.066 −25.145 1.00 20.61 N ATOM 134 CA ALA B 77 4.289 −69.121 −24.655 1.00 21.07 C ATOM 135 C ALA B 77 3.383 −69.298 −25.881 1.00 21.69 C ATOM 136 O ALA B 77 2.567 −68.430 −26.199 1.00 21.93 O ATOM 137 CB ALA B 77 3.937 −67.830 −23.924 1.00 20.10 C ATOM 138 N PRO B 78 3.507 −70.446 −26.564 1.00 22.38 N ATOM 139 CA PRO B 78 2.772 −70.846 −27.771 1.00 20.95 C ATOM 140 C PRO B 78 1.278 −70.535 −27.813 1.00 21.19 C ATOM 141 O PRO B 78 0.789 −69.939 −28.776 1.00 19.68 O ATOM 142 CB PRO B 78 3.027 −72.350 −27.861 1.00 22.21 C ATOM 143 CG PRO B 78 4.288 −72.547 −27.117 1.00 24.07 C ATOM 144 CD PRO B 78 4.211 −71.603 −25.976 1.00 21.89 C ATOM 145 N LEU B 79 0.544 −70.961 −26.790 1.00 21.21 N ATOM 146 CA LEU B 79 −0.896 −70.728 −26.783 1.00 21.32 C ATOM 147 C LEU B 79 −1.275 −69.263 −26.707 1.00 21.17 C ATOM 148 O LEU B 79 −2.125 −68.800 −27.481 1.00 20.44 O ATOM 149 CB LEU B 79 −1.569 −71.476 −25.630 1.00 20.99 C ATOM 150 CG LEU B 79 −1.397 −72.988 −25.617 1.00 22.40 C ATOM 151 CD1 LEU B 79 −2.504 −73.619 −24.772 1.00 22.01 C ATOM 152 CD2 LEU B 79 −1.438 −73.521 −27.021 1.00 23.82 C ATOM 153 N ARG B 80 −0.656 −68.529 −25.788 1.00 20.91 N ATOM 154 CA ARG B 80 −0.980 −67.115 −25.637 1.00 21.30 C ATOM 155 C ARG B 80 −0.526 −66.233 −26.790 1.00 21.29 C ATOM 156 O ARG B 80 −1.278 −65.355 −27.223 1.00 21.47 O ATOM 157 CB ARG B 80 −0.444 −66.583 −24.312 1.00 22.12 C ATOM 158 CG ARG B 80 −1.286 −67.051 −23.118 1.00 24.03 C ATOM 159 CD ARG B 80 −0.610 −66.738 −21.807 1.00 23.42 C ATOM 160 NE ARG B 80 0.581 −67.556 −21.610 1.00 24.59 N ATOM 161 CZ ARG B 80 1.466 −67.351 −20.642 1.00 26.08 C ATOM 162 NH1 ARG B 80 1.290 −66.349 −19.787 1.00 26.92 N ATOM 163 NH2 ARG B 80 2.514 −68.152 −20.519 1.00 27.22 N ATOM 164 N ILE B 81 0.683 −66.448 −27.303 1.00 19.29 N ATOM 165 CA ILE B 81 1.113 −65.621 −28.421 1.00 19.47 C ATOM 166 C ILE B 81 0.256 −65.937 −29.654 1.00 18.99 C ATOM 167 O ILE B 81 −0.149 −65.028 −30.378 1.00 19.38 O ATOM 168 CB ILE B 81 2.639 −65.793 −28.730 1.00 17.92 C ATOM 169 CG1 ILE B 81 3.067 −64.753 −29.769 1.00 18.63 C ATOM 170 CG2 ILE B 81 2.949 −67.200 −29.206 1.00 17.33 C ATOM 171 CD1 ILE B 81 2.746 −63.318 −29.346 1.00 17.46 C ATOM 172 N PHE B 82 −0.056 −67.211 −29.880 1.00 19.39 N ATOM 173 CA PHE B 82 −0.875 −67.582 −31.038 1.00 19.15 C ATOM 174 C PHE B 82 −2.250 −66.931 −30.959 1.00 19.94 C ATOM 175 O PHE B 82 −2.777 −66.444 −31.970 1.00 19.64 O ATOM 176 CB PHE B 82 −1.057 −69.103 −31.136 1.00 19.27 C ATOM 177 CG PHE B 82 −1.811 −69.548 −32.368 1.00 19.87 C ATOM 178 CD1 PHE B 82 −1.180 −69.602 −33.603 1.00 20.87 C ATOM 179 CD2 PHE B 82 −3.154 −69.898 −32.289 1.00 21.11 C ATOM 180 CE1 PHE B 82 −1.872 −70.002 −34.753 1.00 21.20 C ATOM 181 CE2 PHE B 82 −3.857 −70.297 −33.429 1.00 22.26 C ATOM 182 CZ PHE B 82 −3.212 −70.349 −34.663 1.00 22.14 C ATOM 183 N ASN B 83 −2.832 −66.923 −29.764 1.00 19.29 N ATOM 184 CA ASN B 83 −4.150 −66.332 −29.577 1.00 20.90 C ATOM 185 C ASN B 83 −4.178 −64.821 −29.812 1.00 20.83 C ATOM 186 O ASN B 83 −5.086 −64.316 −30.472 1.00 21.92 O ATOM 187 CB ASN B 83 −4.693 −66.641 −28.178 1.00 20.55 C ATOM 188 CG ASN B 83 −6.158 −66.244 −28.028 1.00 22.79 C ATOM 189 OD1 ASN B 83 −6.505 −65.374 −27.229 1.00 25.14 O ATOM 190 ND2 ASN B 83 −7.018 −66.877 −28.807 1.00 20.47 N ATOM 191 N ALA B 84 −3.203 −64.092 −29.275 1.00 19.74 N ATOM 192 CA ALA B 84 −3.177 −62.647 −29.484 1.00 19.30 C ATOM 193 C ALA B 84 −2.967 −62.380 −30.981 1.00 19.94 C ATOM 194 O ALA B 84 −3.561 −61.459 −31.552 1.00 19.69 O ATOM 195 CB ALA B 84 −2.060 −62.008 −28.662 1.00 18.59 C ATOM 196 N TRP B 85 −2.118 −63.197 −31.603 1.00 19.77 N ATOM 197 CA TRP B 85 −1.820 −63.111 −33.032 1.00 20.56 C ATOM 198 C TRP B 85 −3.090 −63.354 −33.865 1.00 21.76 C ATOM 199 O TRP B 85 −3.339 −62.658 −34.859 1.00 20.40 O ATOM 200 CB TRP B 85 −0.754 −64.148 −33.396 1.00 21.46 C ATOM 201 CG TRP B 85 −0.365 −64.167 −34.856 1.00 23.00 C ATOM 202 CD1 TRP B 85 0.301 −63.189 −35.548 1.00 23.17 C ATOM 203 CD2 TRP B 85 −0.588 −65.232 −35.785 1.00 23.69 C ATOM 204 NE1 TRP B 85 0.509 −63.585 −36.848 1.00 24.28 N ATOM 205 CE2 TRP B 85 −0.024 −64.835 −37.022 1.00 24.14 C ATOM 206 CE3 TRP B 85 −1.206 −66.486 −35.693 1.00 24.79 C ATOM 207 CZ2 TRP B 85 −0.060 −65.650 −38.160 1.00 24.90 C ATOM 208 CZ3 TRP B 85 −1.243 −67.299 −36.827 1.00 25.45 C ATOM 209 CH2 TRP B 85 −0.671 −66.875 −38.045 1.00 25.15 C ATOM 210 N ARG B 86 −3.885 −64.346 −33.467 1.00 22.03 N ATOM 211 CA ARG B 86 −5.140 −64.660 −34.166 1.00 23.28 C ATOM 212 C ARG B 86 −6.151 −63.517 −34.007 1.00 22.98 C ATOM 213 O ARG B 86 −6.890 −63.195 −34.942 1.00 21.37 O ATOM 214 CB ARG B 86 −5.754 −65.965 −33.623 1.00 24.72 C ATOM 215 CG ARG B 86 −4.999 −67.236 −34.021 1.00 27.21 C ATOM 216 CD ARG B 86 −5.368 −67.725 −35.418 1.00 29.60 C ATOM 217 NE ARG B 86 −6.626 −68.477 −35.422 1.00 31.45 N ATOM 218 CZ ARG B 86 −7.185 −69.004 −36.508 1.00 31.37 C ATOM 219 NH1 ARG B 86 −6.607 −68.862 −37.696 1.00 32.19 N ATOM 220 NH2 ARG B 86 −8.314 −69.694 −36.405 1.00 31.39 N ATOM 221 N GLN B 87 −6.190 −62.916 −32.821 1.00 22.90 N ATOM 222 CA GLN B 87 −7.101 −61.802 −32.567 1.00 24.07 C ATOM 223 C GLN B 87 −6.738 −60.618 −33.457 1.00 23.85 C ATOM 224 O GLN B 87 −7.613 −60.012 −34.077 1.00 24.02 O ATOM 225 CB GLN B 87 −7.046 −61.382 −31.097 1.00 24.33 C ATOM 226 CG GLN B 87 −7.873 −62.280 −30.187 1.00 27.24 C ATOM 227 CD GLN B 87 −7.720 −61.943 −28.723 1.00 28.81 C ATOM 228 OE1 GLN B 87 −8.567 −62.296 −27.908 1.00 33.25 O ATOM 229 NE2 GLN B 87 −6.632 −61.275 −28.375 1.00 29.95 N ATOM 230 N ALA B 88 −5.449 −60.293 −33.521 1.00 23.39 N ATOM 231 CA ALA B 88 −4.996 −59.183 −34.355 1.00 23.78 C ATOM 232 C ALA B 88 −5.257 −59.485 −35.831 1.00 24.73 C ATOM 233 O ALA B 88 −5.655 −58.595 −36.592 1.00 24.72 O ATOM 234 CB ALA B 88 −3.508 −58.909 −34.116 1.00 23.33 C ATOM 235 N ARG B 89 −5.038 −60.735 −36.244 1.00 24.26 N ATOM 236 CA ARG B 89 −5.285 −61.111 −37.636 1.00 24.94 C ATOM 237 C ARG B 89 −6.752 −60.909 −38.013 1.00 25.29 C ATOM 238 O ARG B 89 −7.056 −60.420 −39.104 1.00 24.27 O ATOM 239 CB ARG B 89 −4.904 −62.575 −37.893 1.00 25.14 C ATOM 240 CG ARG B 89 −3.461 −62.774 −38.353 1.00 24.54 C ATOM 241 CD ARG B 89 −3.142 −64.253 −38.510 1.00 25.50 C ATOM 242 NE ARG B 89 −3.809 −64.901 −39.641 1.00 24.93 N ATOM 243 CZ ARG B 89 −3.329 −64.930 −40.882 1.00 25.90 C ATOM 244 NH1 ARG B 89 −2.178 −64.336 −41.170 1.00 25.98 N ATOM 245 NH2 ARG B 89 −3.979 −65.596 −41.831 1.00 26.36 N ATOM 246 N GLY B 105 5.583 −50.364 −27.741 1.00 23.01 N ATOM 247 CA GLY B 105 4.593 −50.905 −26.827 1.00 23.54 C ATOM 248 C GLY B 105 4.358 −52.380 −27.078 1.00 23.17 C ATOM 249 O GLY B 105 4.449 −52.844 −28.214 1.00 22.69 O ATOM 250 N TYR B 106 4.018 −53.118 −26.026 1.00 22.87 N ATOM 251 CA TYR B 106 3.818 −54.554 −26.159 1.00 22.37 C ATOM 252 C TYR B 106 2.719 −55.018 −27.100 1.00 20.52 C ATOM 253 O TYR B 106 2.867 −56.052 −27.746 1.00 20.50 O ATOM 254 CB TYR B 106 3.632 −55.181 −24.774 1.00 25.08 C ATOM 255 CG TYR B 106 4.864 −55.008 −23.929 1.00 28.19 C ATOM 256 CD1 TYR B 106 4.869 −54.153 −22.830 1.00 31.96 C ATOM 257 CD2 TYR B 106 6.058 −55.631 −24.282 1.00 31.27 C ATOM 258 CE1 TYR B 106 6.043 −53.915 −22.108 1.00 33.13 C ATOM 259 CE2 TYR B 106 7.234 −55.400 −23.569 1.00 32.27 C ATOM 260 CZ TYR B 106 7.219 −54.541 −22.487 1.00 33.19 C ATOM 261 OH TYR B 106 8.388 −54.291 −21.802 1.00 35.95 O ATOM 262 N VAL B 107 1.628 −54.270 −27.205 1.00 19.06 N ATOM 263 CA VAL B 107 0.557 −54.694 −28.099 1.00 18.06 C ATOM 264 C VAL B 107 1.015 −54.743 −29.559 1.00 17.45 C ATOM 265 O VAL B 107 0.502 −55.536 −30.346 1.00 16.99 O ATOM 266 CB VAL B 107 −0.690 −53.774 −27.978 1.00 20.95 C ATOM 267 CG1 VAL B 107 −0.407 −52.407 −28.589 1.00 21.39 C ATOM 268 CG2 VAL B 107 −1.879 −54.433 −28.658 1.00 21.30 C ATOM 269 N SER B 108 1.991 −53.916 −29.918 1.00 17.96 N ATOM 270 CA SER B 108 2.488 −53.892 −31.290 1.00 19.67 C ATOM 271 C SER B 108 3.197 −55.187 −31.694 1.00 20.38 C ATOM 272 O SER B 108 3.385 −55.449 −32.884 1.00 21.25 O ATOM 273 CB SER B 108 3.424 −52.691 −31.508 1.00 19.56 C ATOM 274 OG SER B 108 4.666 −52.824 −30.837 1.00 19.63 O ATOM 275 N GLY B 109 3.595 −55.995 −30.710 1.00 19.59 N ATOM 276 CA GLY B 109 4.251 −57.256 −31.023 1.00 20.03 C ATOM 277 C GLY B 109 3.311 −58.170 −31.792 1.00 19.61 C ATOM 278 O GLY B 109 3.579 −58.517 −32.940 1.00 19.24 O ATOM 279 N PRO B 110 2.206 −58.606 −31.173 1.00 19.20 N ATOM 280 CA PRO B 110 1.251 −59.478 −31.855 1.00 18.99 C ATOM 281 C PRO B 110 0.651 −58.761 −33.075 1.00 19.22 C ATOM 282 O PRO B 110 0.406 −59.371 −34.116 1.00 17.13 O ATOM 283 CB PRO B 110 0.198 −59.737 −30.778 1.00 20.41 C ATOM 284 CG PRO B 110 0.998 −59.720 −29.515 1.00 19.81 C ATOM 285 CD PRO B 110 1.914 −58.528 −29.729 1.00 19.94 C ATOM 286 N GLY B 111 0.407 −57.462 −32.927 1.00 19.03 N ATOM 287 CA GLY B 111 −0.160 −56.702 −34.025 1.00 19.60 C ATOM 288 C GLY B 111 0.764 −56.714 −35.226 1.00 19.59 C ATOM 289 O GLY B 111 0.330 −56.979 −36.339 1.00 21.10 O ATOM 290 N GLY B 112 2.043 −56.429 −34.995 1.00 19.78 N ATOM 291 CA GLY B 112 3.014 −56.417 −36.074 1.00 19.97 C ATOM 292 C GLY B 112 3.147 −57.783 −36.724 1.00 20.43 C ATOM 293 O GLY B 112 3.233 −57.896 −37.949 1.00 19.94 O ATOM 294 N LEU B 113 3.167 −58.828 −35.903 1.00 19.26 N ATOM 295 CA LEU B 113 3.265 −60.184 −36.429 1.00 19.49 C ATOM 296 C LEU B 113 2.040 −60.521 −37.274 1.00 18.73 C ATOM 297 O LEU B 113 2.143 −61.252 −38.255 1.00 18.44 O ATOM 298 CB LEU B 113 3.405 −61.198 −35.289 1.00 18.38 C ATOM 299 CG LEU B 113 4.777 −61.270 −34.605 1.00 20.59 C ATOM 300 CD1 LEU B 113 4.656 −62.059 −33.311 1.00 20.01 C ATOM 301 CD2 LEU B 113 5.794 −61.914 −35.538 1.00 20.23 C ATOM 302 N ALA B 114 0.875 −60.010 −36.892 1.00 18.96 N ATOM 303 CA ALA B 114 −0.334 −60.292 −37.661 1.00 18.70 C ATOM 304 C ALA B 114 −0.288 −59.578 −39.019 1.00 19.30 C ATOM 305 O ALA B 114 −0.602 −60.167 −40.052 1.00 20.62 O ATOM 306 CB ALA B 114 −1.562 −59.855 −36.889 1.00 16.45 C ATOM 307 N ALA B 115 0.082 −58.303 −39.000 1.00 20.57 N ATOM 308 CA ALA B 115 0.167 −57.516 −40.229 1.00 21.84 C ATOM 309 C ALA B 115 1.140 −58.192 −41.189 1.00 21.58 C ATOM 310 O ALA B 115 0.815 −58.464 −42.345 1.00 22.14 O ATOM 311 CB ALA B 115 0.636 −56.108 −39.911 1.00 19.85 C ATOM 312 N TRP B 116 2.334 −58.476 −40.688 1.00 22.12 N ATOM 313 CA TRP B 116 3.365 −59.126 −41.478 1.00 23.22 C ATOM 314 C TRP B 116 2.871 −60.434 −42.123 1.00 23.55 C ATOM 315 O TRP B 116 3.048 −60.643 −43.329 1.00 22.19 O ATOM 316 CB TRP B 116 4.584 −59.367 −40.579 1.00 26.08 C ATOM 317 CG TRP B 116 5.699 −60.136 −41.204 1.00 27.40 C ATOM 316 CD1 TRP B 116 6.473 −59.761 −42.271 1.00 28.30 C ATOM 319 CD2 TRP B 116 6.168 −61.418 −40.793 1.00 28.77 C ATOM 320 NE1 TRP B 116 7.401 −60.742 −42.547 1.00 29.04 N ATOM 321 CE2 TRP B 116 7.234 −61.771 −41.655 1.00 30.37 C ATOM 322 CE3 TRP B 116 5.794 −62.308 −39.778 1.00 30.49 C ATOM 323 CZ2 TRP B 116 7.929 −62.981 −41.529 1.00 31.08 C ATOM 324 CZ3 TRP B 116 6.485 −63.510 −39.653 1.00 31.85 C ATOM 325 CH2 TRP B 116 7.541 −63.834 −40.527 1.00 32.27 C ATOM 326 N SER B 117 2.231 −61.304 −41.338 1.00 21.35 N ATOM 327 CA SER B 117 1.735 −62.573 −41.873 1.00 22.61 C ATOM 328 C SER B 117 0.665 −62.383 −42.940 1.00 23.56 C ATOM 329 O SER B 117 0.463 −63.262 −43.780 1.00 23.11 O ATOM 330 CB SER B 117 1.167 −63.462 −40.756 1.00 20.72 C ATOM 331 OG SER B 117 0.010 −62.889 −40.169 1.00 22.72 O ATOM 332 N LEU B 133 11.788 −52.846 −25.860 1.00 23.38 N ATOM 333 CA LEU B 133 11.903 −54.293 −26.020 1.00 24.54 C ATOM 334 C LEU B 133 11.209 −54.833 −27.276 1.00 22.84 C ATOM 335 O LEU B 133 11.784 −55.619 −28.027 1.00 21.86 O ATOM 336 CB LEU B 133 11.328 −54.996 −24.786 1.00 25.48 C ATOM 337 CG LEU B 133 11.388 −56.527 −24.780 1.00 27.50 C ATOM 338 CD1 LEU B 133 12.840 −56.984 −24.866 1.00 28.69 C ATOM 339 CD2 LEU B 133 10.735 −57.059 −23.509 1.00 28.04 C ATOM 340 N THR B 134 9.975 −54.401 −27.499 1.00 21.72 N ATOM 341 CA THR B 134 9.202 −54.860 −28.639 1.00 21.22 C ATOM 342 C THR B 134 9.693 −54.326 −29.986 1.00 20.62 C ATOM 343 O THR B 134 9.843 −55.091 −30.932 1.00 20.33 O ATOM 344 CB THR B 134 7.716 −54.509 −28.449 1.00 20.99 C ATOM 345 OG1 THR B 134 7.257 −55.075 −27.210 1.00 20.94 O ATOM 346 CG2 THR B 134 6.872 −55.073 −29.600 1.00 20.64 C ATOM 3608 N LYS B 136 12.595 −53.366 −30.809 1.00 21.46 N ATOM 3609 CA LYS B 136 13.886 −53.949 −31.144 1.00 22.79 C ATOM 3610 CB LYS B 136 14.713 −54.196 −29.879 1.00 24.70 C ATOM 3611 CG LYS B 136 16.183 −54.424 −30.178 1.00 27.75 C ATOM 3612 CD LYS B 136 16.998 −54.494 −28.902 1.00 30.17 C ATOM 3613 CE LYS B 136 18.479 −54.671 −29.203 1.00 32.33 C ATOM 3614 NZ LYS B 136 19.278 −54.641 −27.944 1.00 33.37 N ATOM 3615 C LYS B 136 13.793 −55.229 −31.966 1.00 23.46 C ATOM 3616 O LYS B 136 14.561 −55.407 −32.912 1.00 23.71 O ATOM 347 N TRP B 137 12.868 −56.127 −31.633 1.00 21.78 N ATOM 348 CA TRP B 137 12.753 −57.345 −32.424 1.00 22.06 C ATOM 349 C TRP B 137 11.768 −57.202 −33.574 1.00 21.75 C ATOM 350 O TRP B 137 11.936 −57.822 −34.623 1.00 21.76 O ATOM 351 CB TRP B 137 12.361 −58.552 −31.553 1.00 21.20 C ATOM 352 CG TRP B 137 10.990 −58.525 −30.922 1.00 20.23 C ATOM 353 CD1 TRP B 137 10.696 −58.231 −29.618 1.00 19.62 C ATOM 354 CD2 TRP B 137 9.748 −58.877 −31.544 1.00 18.68 C ATOM 355 NE1 TRP B 137 9.349 −58.385 −29.390 1.00 19.31 N ATOM 356 CE2 TRP B 137 8.743 −58.780 −30.555 1.00 18.97 C ATOM 357 CE3 TRP B 137 9.383 −59.270 −32.840 1.00 19.75 C ATOM 358 CZ2 TRP B 137 7.401 −59.058 −30.821 1.00 18.18 C ATOM 359 CZ3 TRP B 137 8.046 −59.549 −33.107 1.00 18.87 C ATOM 360 CH2 TRP B 137 7.072 −59.440 −32.099 1.00 18.94 C ATOM 361 N LEU B 138 10.741 −56.381 −33.386 1.00 21.61 N ATOM 362 CA LEU B 138 9.744 −56.188 −34.431 1.00 23.15 C ATOM 363 C LEU B 138 10.384 −55.558 −35.676 1.00 23.07 C ATOM 364 O LEU B 138 9.958 −55.801 −36.809 1.00 22.68 O ATOM 365 CB LEU B 138 8.618 −55.305 −33.886 1.00 23.87 C ATOM 366 CG LEU B 138 7.312 −55.155 −34.664 1.00 26.48 C ATOM 367 CD1 LEU B 138 6.672 −56.508 −34.915 1.00 25.34 C ATOM 368 CD2 LEU B 138 6.383 −54.267 −33.851 1.00 25.90 C ATOM 3644 N LYS B 140 12.801 −56.332 −37.241 1.00 27.38 N ATOM 3645 CA LYS B 140 13.279 −57.337 −38.182 1.00 28.05 C ATOM 3646 CB LYS B 140 13.893 −58.501 −37.401 1.00 29.91 C ATOM 3647 CG LYS B 140 15.134 −58.057 −36.635 1.00 31.62 C ATOM 3648 CD LYS B 140 15.719 −59.149 −35.757 1.00 33.53 C ATOM 3649 CE LYS B 140 16.974 −58.634 −35.055 1.00 34.46 C ATOM 3650 NZ LYS B 140 17.692 −59.713 −34.320 1.00 36.17 N ATOM 3651 C LYS B 140 12.254 −57.833 −39.212 1.00 27.83 C ATOM 3652 O LYS B 140 12.602 −58.562 −40.142 1.00 27.80 O ATOM 369 N ILE B 141 10.992 −57.445 −39.052 1.00 26.40 N ATOM 370 CA ILE B 141 9.963 −57.818 −40.016 1.00 26.09 C ATOM 371 C ILE B 141 9.316 −56.542 −40.530 1.00 25.81 C ATOM 372 O ILE B 141 8.353 −56.586 −41.305 1.00 26.10 O ATOM 373 CB ILE B 141 8.854 −58.721 −39.405 1.00 26.39 C ATOM 374 CG1 ILE B 141 8.298 −58.092 −38.127 1.00 26.45 C ATOM 375 CG2 ILE B 141 9.401 −60.118 −39.145 1.00 28.33 C ATOM 376 CD1 ILE B 141 7.136 −58.845 −37.549 1.00 26.95 C TER

The following examples are presented for purposes of illustration only and are not intended to limit the scope of the invention in any way.

EXAMPLE 1

This example describes the crystallization of the E. coli MurG protein and the determination of the coordinates of the three-dimensional crystal structure. This example also describes the identification of the donor nucleotide binding site, the acceptor binding site and the membrane association site of the MurG protein.

Abstract

The 1.9 Å X-ray structure of a membrane-associated glycosyltransferase involved in peptidoglycan biosynthesis is reported. This enzyme, MurG, contains two a/B open sheet domains separated by a deep cleft. The C-terminal domain contains the LTDP-GlcNAc binding site while the N-terminal domain contains the acceptor binding site and likely membrane association site. Combined with sequence data from other MurG homologs, this structure provides insight into the residues that are important in substrate binding and catalysis. We have also noted that a conserved region found in many UDP-sugar transferases maps to a β/α/β/α supersecondary structural motif in the donor binding region of MurG, an observation that is be helpful in glycosyltransferase structure prediction.

Methods

Crystallization E. coli MurG containing a C-terminal LEHHHHHHH sequence was purified as described (Ha et al., 1999) and concentrated to 10 mg ml—in 20 mM Tris-HCl, pH 7.9/150 mM NaCl/50 mM EDTA. The protein concentrate was mixed with UDP-GlcNAc in a 1:3 molar ratio. Crystals were grown at room temperature using the hanging-drop vapor-diffusion method by mixing equal volumes of protein with reservoir solution (0.1 M NaMES, pH 6.5/0.96 M (NH,), SO,/0.4% Triton X-100/10 mM DTT). Triclinic crystals with a typical size of 0.2 mm×0.1 mm×0.1 mm grew within a week. The crystals belong to the PI space group, with two molecules per asymmetric unit. The cell dimensions are a=60.613 Å, b=66.356 Å, c=67.902 Å, α=64.294, β=83.520, γ=65.448.

Data Collection and Processing

All data sets were collected at 100 K on previously flash frozen crystals. Crystals were equilibrated in a cryoprotectant buffer with 0.1 M NaMES, pH 6.5, 1.44 M (NH₄)₂SO₄, 0.4% Triton X-100, and 20% glycerol. Heavy-atom soaks were carried out in the same buffer containing one of the following heavy-atom solutions: 2 mM HgCl₂, 1 mM (NH₄)₂WS₄, 1 mM (NH₄)₂OsBr₆. Crystals were flash-frozen in liquid nitrogen. HgC₂ (form A derivative) and (NH₄)₂OsBr₆ derivative data were collected at an R-AX1SIIC imaging plate detector mounted on a Rigaku 200HB generator. Native, HgCl₂ (form B derivative), and (NH₄)₂WS₄ derivative diffraction data were collected at beam-line BioCARS-14B at the Advanced Photon Source, at wavelengths 1.0092 Å, 0.9900 Å and 1.2147 Å respectively. Collection of data on the HgCl₂, derivative was initially designed for MAD phasing; however, the mercury derivative proved to be unstable to X-rays, and after a two-hour exposure to synchrotron radiation the form A derivative metamorphosed into a different mercury derivative (form B) that was suitable for MIR phasing. All the data were reduced using DENZO and SCALEPACK (Otwinowski & Minor, 1997), and processed with CCP4 programs (CCP4, 1994).

Structure Determination and Refinement

The structure was solved by multiple isomorphous replacement combined with anomalous scattering of mercuric derivatives (Table 1). Initial MIR phases calculated with program MLPHARE had a mean figure of merit of 0.44 to 2.5 Å, and were improved by solvent flattening and histogram matching using DM. An MIR map was generated which had continuous electron density for most regions of the protein. A model was built with the program 0 (Jones et al., 1991), and the structure was refined against 1.9 Å data using energy minimization, simulated annealing and B-factor refinement with the program CNS (Brunger et at., 1998). The N-terminal six residues and the C-terminal His-tag had no electron density and were not included in this model. There was no electron density for UDP-GlcNAc.

Results and Discussion

Overall Fold

The crystal structure of E. coli MurG was solved by a combination of multiple isomorphous replacement and anomalous scattering, and refined to 1.9 Å resolution.

TABLE 1 Summary of crystallographic and refinement data Data set Native HgCl₂ (form A derivative) HgCl₂ (form B derivative) (NH₄)₂WS₄ (NH₄)₂OsBr₆ Resolution (Å) 1.9 2.0 1.9 2.4 2.3 Observations 288,150 101,913 245,320 44,366 106,606 Unique reflections 65,567 53,391 65,581 27,950 36,443 R_(sym) ¹ (last shell) 0.032 (0.187) 0.043 (0.200) 0.042 (0.296) 0.031 (0.080) 0.056 (0.302) I/σ (last shell) 41.9 (7.0) 20.4 (2.9) 29.0 (3.7) 24.6 (8.2) 19.6 (2.5) Completeness (last shell) 97.7% (96.4%) 91.4% (66.6%) 97.4% (94.0%) 83.8% (62.0%) 94.3% (78.6%) MIR analysis (40.0-2.5 Å) Mean isomorphous difference² 0.163 0.130 0.068 0.134 Phasing power³ (last shell) 1.09 (0.73) 0.57 (0.50) 0.61 (0.24) 0.61 (0.58) R_(cullis) ⁴ (last shell) 0.81 (0.91) 0.94 (0.96) 0.92 (0.99) 0.94 (0.95) Anomalous R_(cullis) ⁴ (last shell) 0.96 (1.00) 0.95 (1.00) Refinement statistics Resolution 40.0-1.9 Å R.m.s.d.⁷ Reflections (|F| > 2σ) 61,989  Bonds (Å) 0.006 Protein atoms (a.u.) 5,280  Angles (°) 1.29 Water Atoms 298 Sulfate groups 1 Ramachandran plot⁸ R-factor⁵ 22.0%  Residues in most favored region 94.6% R-free⁶ 24.7%   Residues in additional allowed region 5.4% ¹R_(sym) = Σ| I_(i) − <I> |/ΣI_(i), where I_(i) is the intensity of a reflection, and <I> is the average intensity of that reflection. ²Mean isomorphous difference = Σ |F_(PH) − F_(p)|/ΣF_(PH), where F_(PH) and F_(p) are the derivative and native structure factors respectively. ³Phasing power is the ratio of the mean calculated derivative structure factor to the mean lack of closure error. ⁴R_(cullis) is the mean residual lack of closure error divided by the dispersive or anomalous difference. ⁵R-factor = Σ|Fobs| − |Fcalc| |/Σ|F| ⁶R-free is the R-factor calculated using 10% of the reflection data chosen randomly and omitted from the start of refinement. ⁷R.m.s.d., root-mean-square deviations from ideal bond lengths and bond angles. ⁸Calculated with program PROCHECK.

The structure consists of two domains separated by a deep cleft (FIG. 2 a). Both domains exhibit an α/β open-sheet structure and have high structural homology despite minimal sequence homology (RMSD=2.02 over 85 aligned Ca atoms). The N-domain includes residues 7-163 and 341-357, and contains seven parallel β-strands and six α-helices, the last of which originates in the C-domain (FIG. 2 b). The C-domain comprises residues 164-340 and contains six parallel β-strands and eight α-helices, including one irregular bipartite helix (α-link) that connects the N-domain to the first β-strand of the C-domain. The β-strands in both domains are ordered as for a typical Rossman fold. The N- and C-domains are joined by a short linker between the seventh β-strand of the N-domain and the α-link of the C-domain. This inter-domain linker and the peptide segment that joins the last helix of the C-domain to the last helix of the N-domain define the floor of the cleft between the two domains. The cleft itself is about 20 Å deep and 18 Å across at its widest point. Contacts <4 Å across the cleft are limited primarily to interactions between residues from C-α5 to the loop connecting N-β5 to N-α5.

The α/β open-sheet motif (Rossman fold) adopted by both the N- and C-domains of MurG is characteristic of domains that bind nucleotides (Branden & Tooze, 1998). Classical Rossman domains typically contain at least one conserved glycine rich motif, with the consensus sequence GXGXXG, located at a turn between the carboxyl end of one β-strand and the amino terminus of the adjacent α-helix (Baker et al., 1992). This motif is involved in binding the negatively charged phosphates (Carugo & Argos, 1997). There are three glycine rich loops (G loops) in E. coli MurG (FIG. 3 a) that may be variants on the phosphate binding loops found in other dinucleotide binding proteins (see below).

Sequence Homology

Amino acid sequences for eighteen MurG homologs are now available. The sequence similarity between E. coli MurG and homologs from other bacterial strains ranges from less than 30% to more than 90% depending on the evolutionary relationship between the organisms. In all MurG homologs, however, there are several invariant residues. FIG. 3 a shows a sequence alignment for a subset of MurG homologs with the invariant and highly conserved residues indicated. These residues, which include the three G loops, have been highlighted in the E. coli MurG structure (FIG. 3 b). Almost all of the invariant residues are located at or near the cleft between the two domains. Two of the G loops are found in the N domain (between N-β1/N-α1 and N-β4/N-α4) and one is found in the C-domain (between C-β1/C-α1). The strict conservation of the highlighted residues among different bacterial strains, and their location as determined from the E. coli MurG structure, implicates them in substrate binding and catalytic activity.

Structural Homology Reveals the Donor Binding Site

The three-dimensional backbone structure of E. coli MurG was compared to known protein structures, including the three other NDP-glycosyltransferase structures that have been reported (Chamok & Davies, 1999; Gastinel et al., 1999; Vrielink et al., 1994). The C-terminal domain was found to have significant structural homology (RMSD=2.218 Å for 89 aligned C? atoms) to the C-terminal domain of phage T4 β-glucosyltransferase (BGT), an enzyme that catalyzes the glucosylation of hydroxymethyl-cytosines in duplex DNA. A co-crystal structure of BGT with UDP bound in the C-terminal domain reveals the topology of the UDP binding pocket and also shows important contacts to the nucleotide (Morera et al., 1999; Vrielink et al., 1994). These contacts include: a) hydrogen bonds from the backbone amide of 1238 to the N3 and O4 positions of the base; b) hydrogen bonds between the carboxyl side chain of E272 and the O2′ and O3′ hydroxyls of the ribose ring; and c) contacts from a GGS motif in the loop following the first P-strand of the C domain to the alpha phosphate of UDP. The structurally homologous C-domain of MurG contains a topologically similar pocket (FIG. 4 a). Furthermore, even though the two domains share only 11% sequence identity overall, there are identical residues in the same spatial location in E. coli MurG and in BGT. Based on this comparison, we have concluded that the C-domain of E. coli MurG is the UDP-GlcNAc binding site.

We have docked UDP-G1cNAc into the C-domain of E. coli MurG using the information on how UDP binds to BGT as a guide. As shown in FIG. 4 b, the uracil is held in place by contacts from the N3 and 04 atoms to the backbone amide of 1245. The O2′ and O3′ hydroxyls on the ribose sugar arc within hydrogen bonding distance of the invariant glutamate residue (E269) in the middle of helix C-?4. The conserved GGS motif in G loop 3 is positioned to contact the alpha phosphate. When these contacts are made, the UDP-GlcNAc substrate fits nicely into a pocket in the C-domain, where it is surrounded by many of the invariant residues identified through sequence analysis of other MurG homologs. It is possible to propose roles for some of these invariant residues from the model. For example, the side chain of R261 can be rotated to contact the second phosphate; this contact may help explain why UDP binds significantly better to MurG than UMP. We propose that R261 plays an important role in catalysis by stabilizing the UDP leaving group via electrostatic interactions. The side chain of Q289 is within hydrogen bonding distance of the C4 hydroxyl of the GlcNAc sugar. This contact may explain why MurG can discriminate between UDP-G1cNAc and its C4 axial isomer, UDP-GalNAc (Ha et at., 1999).

The Acceptor Binding Site

Structural considerations suggest that the primary acceptor binding site is located in the N-terminal domain of MurG. This domain contains three highly conserved regions, two of which are glycine-rich loops that face the cleft (FIGS. 3 a and 4 c). These G loops are reminiscent of the phosphate binding loops found in other nucleotide binding proteins, and are most likely involved in binding to the diphosphate on Lipid I. The N-termini of the helices following each G loop form opposite walls of a small pocket between the G loops. The helix dipoles create a positively charged electrostatic field in the pocket that can stabilize the negative charged diphosphates. When the diphosphate of the acceptor is anchored in the pocket created by the G-loops, the MurNAc sugar emerges into the cleft between domains and the C4 hydroxyl can be directed towards the anomeric carbon of the G1cNAc for attack on the face opposite the UDP leaving group. The third conserved region in the N domain spans the loop from the end of N-?5 to the middle of N-?5. Kinetic analysis of mutants is required to evaluate the roles of these residues (Ha et al., 1999; Men et al., 1998).

Proposed Membrane Association Site

MurG associates with the cytoplasmic surface of bacterial membranes where it couples a soluble donor sugar to the membrane anchored acceptor sugar, Lipid I. Analysis of the E. coli MurG structure shows that there is a hydrophobic patch consisting of residues 175, L79, F82, W85 and W116 in the N-domain, which is surrounded by basic residues (K72, K140, K69, R80, R86, R89). We propose that this is the membrane association site and that association involves both hydrophobic and electrostatic interactions with the negatively charged bacterial membrane. The location of this patch in MurG is also consistent with the proposed acceptor binding site: membrane association at this patch would bring the two N-terminal G loops close to the membrane surface where the diphosphate portion of the acceptor is located (FIG. 4 c). Moreover, the cleft between the two domains would remain accessible, consistent with the biochemical requirement that the soluble UDP-GlcNAc donor be able to find its binding site from the cytoplasm.

Implications for Other Glycosyltransferases

Glycosyltransferases that utilize an activated nucleotide sugar as a donor comprise a large family of enzymes in both prokaryotes and eukaryotes, and they play central roles in many important biological processes (Dennis et al., 1999; Koya et al., 1999; Verbert & Cacan, 1999). Glycosyltransferases are typically classified according to the nucleotide sugar they utilize, and it has frequently been noted that there is no significant sequence homology even among glycosyltransferases in the same family. This has made it difficult to identify common structural features and residues important in binding and catalysis. There are only three other glycosyltransferase structures available, and although none of them shows any sequence homology to MurG, a structural comparison indicates that one of them, BGT, contains a related donor binding site.

In addition to this structural homology, we have identified a strikingly similar sequence motif in the MurG family and certain other UDP-glycosyltransferase families. This sequence motif spans about a thirty amino acid stretch in the C-domain of MurG and includes most of the invariant residues found in that domain. As shown in FIG. 3 a, a similar motif is found in the UDP-glucuronosyltransferases (Mackenzie, 1990). Certain residues are identical, including a number of prolines and glycines, and the spacing between them is invariant. This suggests that the UDP-glucuronosyltransferases contain a region of α/β supersecondary structure that is involved in a similar function as the corresponding region in MurG (FIG. 3 c). This region binds the donor sugar. By analyzing the similarities and differences between the conserved residues in this subdomain in the MurG family and other UDP-glycosyltransferase families, it may be possible to identify—and perhaps alter—residues that are involved in determining donor selectivity. We note that it would be useful to be able to manipulate donor specificity because it would extend the utility of glycosyltransferases as reagents for glycosylation of complex molecules. Altered glycosyltransferases could also be useful for remodeling cell surfaces and for probing the biological roles of particular carbohydrate structures.

Conclusion

This first structure of a member of the MurG family of glycosyltransferases lays the groundwork for further mechanistic and structural investigations, which may lead to the design of inhibitors and perhaps even new antibiotics. The work also shows that there can be conserved subdomains even in very different glycosyltransferase families. Information on conserved subdomains will be useful for structure prediction and may help guide experiments directed towards changing substrate specificity.

EXAMPLE 2

This example describes a method of isolating the C-terminal domain of the E. coli MurG protein, expressing the domain in E. coli cells and utilizing nuclear magnetic resonance (NMR) to determine the ability of compounds to bind.

MurG can also be used to determine the ability of a chemical compound to bind to the C domain by a) determining the start of c domain based on the MurG crystal structure; b) independently expressing the C domain; and c) using NMR methods to identify binding site and/or bound conformation of ligand. The same procedure is used for the acceptor binding domains.

NMR methods are used to identify the protein binding sites and screen for ligands that bind. The MurG C-terminal domain region of the protein has been expressed independently. The C domain has a much lower molecular weight than the full-length protein. Therefore, the expression of the C domain results in much sharper NMR peaks which will facilitate the NMR interpretation. Also the proton chemical shifts are very sensitive to their environment. Binding of a compound will introduce local environment changes, thus changing the proton chemical shifts. In this way, residues involved in the binding can be differentiated easily from other amino-acid residues not involved in binding a ligand. This method has also been used to identify ligands that bind to low molecular weight drug targets (i.e., small proteins).

Relevant references to NMR techniques are: Discovering high-affinity ligands for proteins: SAR by NMR, S. Shuker, P. Hajduk, R. Meadows, and S. Fesik, Science 274, 1531 (1996); Lin Y, Nageswara Rao B D. Structural characterization of adenine nucleotides bound to Escherichia coli adenylate kinase. I. Adenosineconformations by proton two-dimensional transferred nuclear Overhauser effect spectroscopy. Biochemistry. 2000 Apr. 4;39(13):3636-46; and Fejzo J, et al., Chem Biol October 1999 6(10):755-69 (incorporated herein by reference).

The SHAPES strategy is also useful for NMR identification of binding residues, ligands and drug discover which is an NMR-based approach for lead generation in drug discovery. Recently, it has been shown that nuclear magnetic resonance (NMR) may be used to identify ligands that bind to low molecular weight protein drugtargets. Recognizing the utility of NMR as a very sensitive method for detecting binding, we have focused on developing alternative approaches that are applicable to larger molecular weight drug targets and do not require isotopic labeling. A new method for lead generation (SHAPES) uses NMR to detect the binding of a limited but diverse library of small molecules to a potential drug target. The compound scaffolds are derived from shapes most commonly found in known therapeutic agents. NMR detection of low (microM-mM) affinity binding is achieved using either differential line broadening or transferred NOE (nuclear Overhauser effect) NMR techniques. The SHAPES method for lead generation by NMR is useful for identifying potential lead classes of drugs early in a drug design program, and is easily integrated with other discovery tools such as virtual screening, high-throughput screening and combinatorial chemistry.

EXAMPLE 3

This example describes the method of using the three-dimensional structure of E. coli MurG to determine the crystal structures of its mutant, enzyme-ligand complex, and MurG homologs, which share the same folding motif.

First, a crystalline form of the new protein or the protein complex should be obtained. The E. coli MurG mutants should be crystallized in a condition very similar to what we have showed in the method section. The protein-ligand complex can be obtained by soaking the protein crystals in a ligand-containing buffer. Other MurG homologs can be expressed in a His-tagged fashion and purified using affinity colume. Presumably they can be crystallized in a similar way using a detergent as the additive. Next, the diffraction data should be collected and processed. After the data collection, the molecular replacement method is used to determine the unknown structure. Either the whole E. coli MurG protein or one single domain can serve as a search model. This search model can be rotated and translated until the correct orientation is located in the unit cell of this unknown structure. The search model may only represent part of the contents of the asymmetric unit. However, the location of the first model is now already available. While the first location of the search model is fixed, the second round of translation search can be carried out to search more molecules or domains in the asymmetric unit cell. The phases from the final model generated by molecular replacement can be used to calculate the electron density map. Finally, a model is built based on the electron density map, and the model needs to be refined using program CNS or XPLOR.

EXAMPLE 4

This example describes the method of using the three-dimensional coordinate structure of E. coli MurG to produce a protein fragment that can be used in an NMR-based lead discovery program. The crystal structure reveals the boundaries of the C domain and permits us to design a gene containing only the C domain from the gene containing both domains. The C domain starting at residue 164 and ending at residue 340 was cloned into an expression vector to generate a C-terminal His-tag fusion, It was over-expressed in E. coli cells and purified by affinity colume. The protein was shown to be monomeric by size exclusion chromatography and to be soluble at least up to 0.15 mM, a concentration more than adequate for NMR analysis. C domains from other MurG homologues can be similarly expressed and used.

EXAMPLE 5

This example describes the co-crystallization of a MurG protein with a ligand. A MurG-ligand complex is formed by either co-crystallizing MurG protein with appropriate ligand or soaking the MurG crystals in buffers containing appropriate ligand. Co-crystallization is done by pre-mixing the protein sample with a certain amount of substrate or substrate analogs. Then the hanging drop method is used to produce crystals as described infra.

Alternatively, ligans are incorporated into the crystals by soaking the protein crystals in the ligand containing buffer for a period of time to allow for infiltration into the crystal. The time ranges from a couple of hours to a couple of days. The concentration of ligand in the buffer ranges from several milimolar to several hundred mili molar.

Deposit of Coordinates

The crystal structure three-dimensional coordinates of the E. coli MurG as set forth in Table 1 were deposited with the Protein Data Bank and hare been assigned the indicated ID Code (Accession No.) 1F0K.

Although the invention is described in detail with reference to specific embodiments thereof, it will be understood that variations which are functionally equivalent are within the scope of this invention. Indeed, various modifications of the invention in addition to those shown and described herein will become apparent to those skilled in the art from the foregoing description and accompanying drawings. Such modifications are intended to fall within the scope of the appended claims.

Various publications are cited herein, the disclosures of which are incorporated by reference in their entireties.

REFERENCES

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1. A method of obtaining a triclinic crystal composition of the bacterial membrane associated UDP-glycosyltransferase of SEQ ID NO: 1 (MurG protein), said method consisting of: (a) preparing a solution containing 10 mg/ml of MurG protein in 20 mM Tris-HCl buffer, pH 7.9, 150 mM NaCl, 50 mM EDTA, and three molar equivalent of UDP-GlcNAc to the MurG protein; and (b) growing a triclinic crystal at room temperature using the hanging drop-method by mixing equal volumes of the protein solution of (a) with a reservoir solution consisting of 0.1 M NaMES, pH 6.5, 0.96 M ammonium sulfate, 0.4% Triton X-100, and 10 mM DTT.
 2. A crystalline composition produced according to the method of claim
 1. 3. A crystalline composition according to claim 2 comprising MurG crystal molecules arranged in a P1 space group with two molecules per asymmetric unit so as to form a unit cell of dimensions a=60.613 Å, b=66.356 Å, c=67.902 Å, α=64.294°, β=83.520°, and γ=65.448°. 